Research workbench
Crystal structure of human BRR2 in complex with T-3905516
Analyse Crystal structure of human BRR2 in complex with T-3905516 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5URJ
- Type
- protein
- Length
- 1,707 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- U5 small nuclear ribonucleoprotein 200 kda helicase
- EC
- 3.6.4.13
- UniProt
- O75643
- Ligands
- 8LS
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | U5 small nuclear ribonucleoprotein 200 kda helicase (EC 3.6.4.13) | protein | 1707 | 43% helix, 17% strand | O75643 |
Ligands and binding sites
- 8LS · 6-benzyl-3-[(2R)-2-(3-fluoropyridin-2-yl)-6-methyl-3,4-dihydro-2H-1-benzopyran-7-yl]-4,6-dihydropyrido[4,3-d]pyrimidine-2,7(3H,8H)-dione · ligand · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 639 | 0.81 | 0.85 | 67 | GOL, 8LS |
| 2 | 1053 | 0.79 | 0.80 | 86 | empty |
| 3 | 394 | 0.76 | 0.86 | 60 | empty |
| 4 | 509 | 0.76 | 0.84 | 65 | empty |
| 5 | 694 | 0.74 | 0.80 | 48 | empty |
Compared structures
- 5URJ · Crystal structure of human BRR2 in complex with T-3905516 · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O75643
- Elsewhere: RCSB PDB 5URJ · PDBe 5URJ · UniProt O75643
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