UniProt O14744
Protein arginine N-methyltransferase 5 (O14744)
Protein arginine N-methyltransferase 5 (UniProt O14744), EC 2.1.1.-, 2.1.1.125: 105 experimental structures and 1 predicted model on GenesisL1, 55 ligands bound, 521 pockets. Binding sites, druggability and experiment against…
- UniProt
- O14744
- Protein
- Protein arginine N-methyltransferase 5
- EC
- 2.1.1.-, 2.1.1.125, 2.1.1.320
- Experimental structures
- 105
- Predicted models
- 1
- Ligands
- 55
- Pockets
- 521 · 74 records with a druggable one
Structures
106 records of O14744 in the MolNFT archive: 105 experimental, 1 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 4GQB | Crystal Structure of the human PRMT5:MEP50 Complex | x-ray diffraction | A | 0XU | 7 (best 0.85) |
| 4GQB | Crystal structure of the human PRMT5:MEP50 complex | x-ray diffraction | A | ACE, 0XU | 7 (best 0.85) |
| 4X60 | Crystal structure of PRMT5:MEP50 with EPZ015666 and sinefungin | x-ray diffraction | A | SFG, 3XV | 7 (best 0.84) |
| 4X60 | Crystal structure of PRMT5:MEP50 with EPZ015666 and sinefungin | x-ray diffraction | A | SFG, 3XV | 7 (best 0.84) |
| 4X61 | Crystal structure of PRMT5:MEP50 with EPZ015666 and SAM | x-ray diffraction | A | SAM, 3XV | 6 (best 0.85) |
| 4X61 | Crystal structure of PRMT5:MEP50 with EPZ015666 and SAM | x-ray diffraction | A | SAM, 3XV | 6 (best 0.85) |
| 4X63 | Crystal structure of PRMT5:MEP50 with EPZ015666 and SAH | x-ray diffraction | A | SAH, 3XV | 6 (best 0.85) |
| 4X63 | Crystal structure of PRMT5:MEP50 with EPZ015666 and sah | x-ray diffraction | A | SAH, 3XV | 6 (best 0.85) |
| 5C9Z | Crystal structure of PRMT5:MEP50 with EPZ015866 and sinefungin | x-ray diffraction | A | SFG, 4Z2 | 6 (best 0.84) |
| 5C9Z | Crystal structure of PRMT5:MEP50 with EPZ015866 and sinefungin | x-ray diffraction | A | SFG, 4Z2 | 6 (best 0.84) |
| 5EMJ | Crystal structure of PRMT5:MEP50 with Compound 8 and sinefungin | x-ray diffraction | A | SFG, 5QJ | 6 (best 0.84) |
| 5EMJ | Crystal structure of PRMT5:MEP50 with compound 8 and sinefungin | x-ray diffraction | A | SFG, 5QJ | 6 (best 0.84) |
| 5EMK | Crystal structure of PRMT5:MEP50 with Compound 9 and sinefungin | x-ray diffraction | A | SFG, 5QH | 6 (best 0.84) |
| 5EMK | Crystal structure of PRMT5:MEP50 with compound 9 and sinefungin | x-ray diffraction | A | SFG, 5QH | 6 (best 0.84) |
| 5EML | Crystal structure of PRMT5:MEP50 with Compound 10 and SAM | x-ray diffraction | A | SAM, 5QK | 9 (best 0.84) |
| 5EML | Crystal structure of PRMT5:MEP50 with compound 10 and SAM | x-ray diffraction | A | SAM, 5QK | 9 (best 0.84) |
| 5EMM | Crystal structure of PRMT5:MEP50 with Compound 15 and sinefungin | x-ray diffraction | A | SFG, 5QL | 6 (best 0.85) |
| 5EMM | Crystal structure of PRMT5:MEP50 with compound 15 and sinefungin | x-ray diffraction | A | SFG, 5QL | 6 (best 0.85) |
| 5FA5 | Crystal Structure of PRMT5:MEP50 in complex with MTA and H4 peptide | x-ray diffraction | A | MTA | 6 (best 0.88) |
| 5FA5 | Crystal structure of PRMT5:MEP50 in complex with mta and H4 peptide | x-ray diffraction | A | MTA | 6 (best 0.88) |
| 6CKC | Structure of PRMT5:MEP50 in complex with LLY-283, a potent and selective inhibitor of PRMT5, with… | x-ray diffraction | A | F5J | 7 (best 0.84) |
| 6CKC | Structure of PRMT5:MEP50 in complex with lly-283, a potent and selective inhibitor of PRMT5, with… | x-ray diffraction | A | F5J | — |
| 6K1S | Discovery of Potent and Selective Covalent Protein Arginine Methyltransferase (PRMT5) Inhibitors | x-ray diffraction | A | CUX | 6 (best 0.85) |
| 6K1S | Discovery of potent and selective covalent protein arginine methyltransferase (PRMT5) inhibitors | x-ray diffraction | A | CUX | — |
| 6RLL | CRYSTAL STRUCTURE OF THE HUMAN PRMT5:MEP50 COMPLEX with JNJ44064146 | x-ray diffraction | A | K8H | 6 (best 0.88) |
| 6RLL | Crystal structure of the human PRMT5:MEP50 complex with JNJ44064146 | x-ray diffraction | A | K8H | — |
| 6RLQ | CRYSTAL STRUCTURE OF THE HUMAN PRMT5:MEP50 COMPLEX with JNJ45031882 | x-ray diffraction | A | K8N | 7 (best 0.84) |
| 6RLQ | Crystal structure of the human PRMT5:MEP50 complex with JNJ45031882 | x-ray diffraction | A | K8N | — |
| 6UGH | Cryo-EM structure of the apo form of human PRMT5:MEP50 complex at a resolution of 3.4 angstrom | electron microscopy | A | — | 5 (best 0.82) |
| 6UGH | Cryo-EM structure of the apo form of human PRMT5:MEP50 complex at a resolution of 3.4 ångström | electron microscopy | A | — | — |
| 6UXX | PRMT5:MEP50 Complexed with Allosteric Inhibitor Compound 1a | x-ray diffraction | A | QL1 | 8 (best 0.84) |
| 6UXX | PRMT5:MEP50 complexed with allosteric inhibitor compound 1A | x-ray diffraction | A | QL1 | — |
| 6UXY | PRMT5:MEP50 Complexed with Allosteric Inhibitor Compound 8 | x-ray diffraction | A | QKY | 9 (best 0.84) |
| 6UXY | PRMT5:MEP50 complexed with allosteric inhibitor compound 8 | x-ray diffraction | A | QKY | — |
| 6V0N | PRMT5 bound to PBM peptide from Riok1 | x-ray diffraction | A | SFG | 6 (best 0.85) |
| 6V0N | PRMT5 bound to pbm peptide from RIOK1 | x-ray diffraction | A | — | — |
| 6V0O | PRMT5 bound to the PBM peptide from pICln | x-ray diffraction | A | SFG, ACE | 7 (best 0.85) |
| 6V0O | PRMT5 bound to the pbm peptide from picln | x-ray diffraction | A | ACE | — |
| 6V0P | PRMT5 complex bound to covalent PBM inhibitor BRD6711 | x-ray diffraction | A | QN4, CL, SFG | 6 (best 0.88) |
| 6V0P | PRMT5 complex bound to covalent pbm inhibitor BRD6711 | x-ray diffraction | A | QN4, CL | — |
| 7BO7 | CRYSTAL STRUCTURE OF THE HUMAN PRMT5:MEP50 COMPLEX with JNJB44355437 | x-ray diffraction | AAA | U6K | 7 (best 0.85) |
| 7BOC | Crystal structure of the PRMT5 TIM barrel domain in complex with RioK1 peptide | x-ray diffraction | A | — | 1 (best 0.40) |
| 7BOC | Crystal structure of the PRMT5 tim barrel domain in complex with RIOK1 peptide | x-ray diffraction | A | — | — |
| 7KIB | PRMT5:MEP50 Complexed with 5,5-Bicyclic Inhibitor Compound 4 | x-ray diffraction | A | WFM, CL | 6 (best 0.85) |
| 7KIB | PRMT5:MEP50 complexed with 5,5-bicyclic inhibitor compound 4 | x-ray diffraction | A | WFM, CL | — |
| 7KIC | PRMT5:MEP50 Complexed with 5,5-Bicyclic Inhibitor Compound 34 | x-ray diffraction | A | WFS | 6 (best 0.85) |
| 7KIC | PRMT5:MEP50 complexed with 5,5-bicyclic inhibitor compound 34 | x-ray diffraction | A | WFS | — |
| 7KID | PRMT5:MEP50 Complexed with 5,5-Bicyclic Inhibitor Compound 72 | x-ray diffraction | A | WFV | 6 (best 0.87) |
| 7KID | PRMT5:MEP50 complexed with 5,5-bicyclic inhibitor compound 72 | x-ray diffraction | A | WFV | — |
| 7L1G | PRMT5-MEP50 Complexed with SAM | x-ray diffraction | A | CL, SAM | 7 (best 0.85) |
| 7L1G | PRMT5-MEP50 complexed with SAM | x-ray diffraction | A | CL | — |
| 7M05 | CryoEM structure of PRMT5 bound to covalent PBM-site inhibitor BRD-6988 | electron microscopy | A, C, E, G | YJG | 20 (best 0.85) |
| 7M05 | Cryoem structure of PRMT5 bound to covalent pbm-site inhibitor brd- 6988 | electron microscopy | A, C, E, G | YJG | — |
| 7MX7 | PRMT5:MEP50 complexed with inhibitor PF-06939999 | x-ray diffraction | A | ZR1 | 5 (best 0.83) |
| 7MX7 | PRMT5:MEP50 complexed with inhibitor pf-06939999 | x-ray diffraction | A | ZR1 | — |
| 7MXA | PRMT5:MEP50 complexed with inhibitor PF-06855800 | x-ray diffraction | A | ZR4 | 7 (best 0.83) |
| 7MXA | PRMT5:MEP50 complexed with inhibitor pf-06855800 | x-ray diffraction | A | ZR4 | — |
| 7MXC | PRMT5:MEP50 complexed with adenosine | x-ray diffraction | A | ADN | 9 (best 0.84) |
| 7MXC | PRMT5:MEP50 complexed with adenosine | x-ray diffraction | A | ADN | — |
| 7MXG | PRMT5(M420T mutant):MEP50 complexed with inhibitor PF-06855800 | x-ray diffraction | A, C | ZR4 | 16 (best 0.83) |
46 records more on the page itself.
Ligands
- MTA · 5'-deoxy-5'-methylthioadenosine · in 39 records
- CL · Chloride ion · in 15 records
- SFG · Sinefungin · in 14 records
- 3XV · N-[(2S)-3-(3,4-dihydroisoquinolin-2(1H)-yl)-2-hydroxypropyl]-6-(oxetan-3-ylamino)pyrimidine-4-carboxamide · in 6 records
- UNL · Unknown ligand · in 6 records
- SAM · S-adenosylmethionine · in 5 records
- SO4 · Sulfate ion · in 5 records
- ZR1 · (1S,2S,3S,5R)-3-{[6-(difluoromethyl)-5-fluoro-1,2,3,4-tetrahydroisoquinolin-8-yl]oxy}-5-(4-methyl-7H-pyrrolo[2,3-d]pyrimidin-7-yl)cyclopentane-1,2-diol · in 4 records
- ZR4 · 7-[(5R)-5-C-(4-chloro-3-fluorophenyl)-beta-D-ribofuranosyl]-7H-pyrrolo[2,3-d]pyrimidin-4-amine · in 4 records
- ACE · Acetyl group · in 3 records
- ADN · Adenosine · in 3 records
- 0XU · (2S,5S,6E)-2,5-diamino-6-[(3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxydihydrofuran-2(3H)-ylidene]hexanoic acid · in 2 records
- 4Z2 · 2-(cyclobutylamino)-N-[(2S)-3-(3,4-dihydroisoquinolin-2(1H)-yl)-2-hydroxypropyl]pyridine-4-carboxamide · in 2 records
- 5QH · ~{N}-[(2~{S})-3-(3,4-dihydro-1~{H}-isoquinolin-2-yl)-2-oxidanyl-propyl]-3-pyridin-2-yl-benzamide · in 2 records
- 5QJ · (2~{S})-1-(3,4-dihydro-1~{H}-isoquinolin-2-yl)-3-[[4-(3-methylbenzimidazol-5-yl)pyridin-2-yl]amino]propan-2-ol · in 2 records
- 5QK · ~{N}-[(2~{R})-3-(3,4-dihydro-1~{H}-isoquinolin-2-yl)-2-oxidanyl-propyl]-2-quinolin-8-yloxy-ethanamide · in 2 records
- 5QL · ~{N}-[(2~{S})-3-(3,4-dihydro-1~{H}-isoquinolin-2-yl)-2-oxidanyl-propyl]-3-(oxan-4-ylamino)benzamide · in 2 records
- 81X · 4-(aminomethyl)phthalazin-1(2H)-one · in 2 records
- 84W · [7-(1-methyl-1H-pyrazol-4-yl)-4-oxo-3,4-dihydrophthalazin-1-yl]methanaminium · in 2 records
- 85E · {7-[(5M)-5-(1-cyano-3-fluoronaphthalen-2-yl)-1-methyl-1H-pyrazol-4-yl]-4-oxo-3,4-dihydrophthalazin-1-yl}methanaminium · in 2 records
- 85K · (7-{(5M)-5-[3-chloro-6-cyano-5-(cyclopropyloxy)-2-fluorophenyl]-1-methyl-1H-pyrazol-4-yl}-4-oxo-3,4-dihydrophthalazin-1-yl)methanaminium · in 2 records
- 97L · (2M)-2-{4-[4-(aminomethyl)-1-oxo-1,2-dihydrophthalazin-6-yl]-1-methyl-1H-pyrazol-5-yl}-1-benzothiophene-3-carbonitrile · in 2 records
- 97X · (2P)-2-{4-[4-(aminomethyl)-1-oxo-1,2-dihydrophthalazin-6-yl]-1-methyl-1H-pyrazol-5-yl}naphthalene-1-carbonitrile · in 2 records
- CUX · 2-[[7-[(2~{R},3~{R},4~{S},5~{R})-5-[(~{R})-(4-chlorophenyl)-oxidanyl-methyl]-3,4-bis(oxidanyl) oxolan-2-yl]pyrrolo[2,3-d]pyrimidin-4-yl]amino]ethanal · in 2 records
- F5J · 7-[(5R)-5-C-phenyl-beta-D-ribofuranosyl]-7H-pyrrolo[2, 3-d]pyrimidin-4-amine · in 2 records
- K8H · (2~{R},3~{R},4~{S},5~{R})-2-(4-azanylpyrrolo[2,3-d]pyrimidin-7-yl)-5-(1,8-diazaspiro[4.5]decan-1-ylmethyl)oxolane-3,4-diol · in 2 records
- K8N · (1~{S},2~{R},3~{S},5~{R})-3-[2-(2-azanyl-3-bromanyl-quinolin-7-yl)ethyl]-5-(4-azanylpyrrolo[2,3-d]pyrimidin-7-yl)cyclop entane-1,2-diol · in 2 records
- LB3 · (9R,10R,11S,12R,13R,14R)-4-amino-9-(3,4-difluorophenyl)-6,7,8,9,10,11,12,13-octahydro-10,13-epoxy[1,3]diazecino[1,2-e]purine-11,12-diol · in 2 records
- NA · Sodium ion · in 2 records
- NXF · (2M)-2-[(4M)-4-{4-(aminomethyl)-1-oxo-8-[(2R)-oxolan-2-yl]-1,2-dihydrophthalazin-6-yl}-1-methyl-1H-pyrazol-5-yl]-1-benzothiophene-3-carbonitrile · in 2 records
Experiment against prediction
- 8G1U chain E against the predicted model O14744: TM-score 0.99, RMSD 1.09 Å
- 8G1U chain M against the predicted model O14744: TM-score 0.99, RMSD 1.08 Å
- 8G1U chain I against the predicted model O14744: TM-score 0.99, RMSD 1.11 Å
- 8G1U chain A against the predicted model O14744: TM-score 0.98, RMSD 1.09 Å
- 6UGH chain A against the predicted model O14744: TM-score 0.98, RMSD 1.16 Å
- 6UGH chain A against the predicted model O14744: TM-score 0.98, RMSD 1.16 Å
- 6RLL chain A against the predicted model O14744: TM-score 0.98, RMSD 1.48 Å
- 6RLL chain A against the predicted model O14744: TM-score 0.98, RMSD 1.48 Å
- 6V0P chain A against the predicted model O14744: TM-score 0.98, RMSD 1.58 Å
- 9EYV chain A against the predicted model O14744: TM-score 0.98, RMSD 1.60 Å
Elsewhere
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