UniProt Q9HU22
Glucose-1-phosphate thymidylyltransferase (Q9HU22)
Glucose-1-phosphate thymidylyltransferase (UniProt Q9HU22), EC 2.7.7.24: 35 experimental structures on GenesisL1, 6 ligands bound, 20 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- Q9HU22
- Protein
- Glucose-1-phosphate thymidylyltransferase
- EC
- 2.7.7.24
- Experimental structures
- 35
- Predicted models
- 0
- Ligands
- 6
- Pockets
- 20 · 1 record with a druggable one
Structures
35 records of Q9HU22 in the MolNFT archive: 35 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 1FXO | The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 1FXO | The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 1FZW | The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 1FZW | The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 1G0R | The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 1G0R | The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 1G1L | The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 1G1L | The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 1G23 | The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 1G23 | The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 1G2V | The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 1G2V | The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 1G3L | The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate… | x-ray diffraction | A, B, C, D | — | — |
| 1G3L | The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate… | x-ray diffraction | A, B, C, D | — | — |
| 4B2X | Pseudomonas aeruginosa RmlA in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | — | — |
| 4B2X | Pseudomonas aeruginosa rmla in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | — | — |
| 4B3U | Pseudomonas aeruginosa RmlA in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | — | — |
| 4B3U | Pseudomonas aeruginosa rmla in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | — | — |
| 4B4B | Pseudomonas aeruginosa RmlA in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | — | — |
| 4B4B | Pseudomonas aeruginosa rmla in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | — | — |
| 4B4G | Pseudomonas aeruginosa RmlA in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | — | — |
| 4B4G | Pseudomonas aeruginosa rmla in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | — | — |
| 4B4M | Pseudomonas aeruginosa RmlA in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | — | — |
| 4B4M | Pseudomonas aeruginosa rmla in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | — | — |
| 4B5B | Pseudomonas aeruginosa RmlA in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | — | — |
| 4B5B | Pseudomonas aeruginosa rmla in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | — | — |
| 5FTS | Pseudomonas aeruginosa RmlA in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | P3I, CL | 20 (best 0.81) |
| 5FTS | Pseudomonas aeruginosa rmla in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | — | — |
| 5FTV | Pseudomonas aeruginosa rmla in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | — | — |
| 5FU0 | Pseudomonas aeruginosa RmlA in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | FKH, CL | — |
| 5FU0 | Pseudomonas aeruginosa rmla in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | — | — |
| 5FU8 | Pseudomonas aeruginosa RmlA in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | DH5, CL | — |
| 5FU8 | Pseudomonas aeruginosa rmla in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | — | — |
| 5FUH | Pseudomonas aeruginosa rmla in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | — | — |
| 6T38 | Pseudomonas aeruginosa rmla in complex with allosteric inhibitor | x-ray diffraction | A, B, C, D | MBK, BR, CL | — |
Ligands
- CL · Chloride ion · in 4 records
- BR · Bromide ion · in 1 record
- DH5 · N-(6-amino-1-(4-bromo-3-methylbenzyl)-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-methylbenzenesulfonamide · in 1 record
- FKH · N-(6-amino-1-(3-methylbenzyl)-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-methylbenzenesulfonamide · in 1 record
- MBK · ~{N}-[6-(4-azanylbutylamino)-1-[(4-bromophenyl)methyl]-2,4-bis(oxidanylidene)pyrimidin-5-yl]-~{N}-methyl-benzenesulfonamide · in 1 record
- P3I · N-(6-Amino-1-(2-bromobenzyl)-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-methylbenzenesulfonamide · in 1 record
Elsewhere
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