MolNFT v1 · #7317 · protein
GP31 co-chaperonin from bacteriophage T4
1G31: “GP31 co-chaperonin from bacteriophage T4”. X-ray diffraction, 2 ligands (K, PO4), 10 pockets (best druggability 0.55). MolNFT v1 #7317 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1G31
- Type
- protein
- Length
- 749 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GP31
- UniProt
- P17313
- Ligands
- K, PO4
- Pockets
- 10 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | GP31 | protein | 107 | 21% helix, 30% strand | P17313 |
Ligands and binding sites
- K · Potassium ion · metal · 11 copies · chains A, B, C, D, E, F, G
- PO4 · Phosphate ion · ion · 19 copies · chains G, A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 304 | 0.55 | 0.75 | 42 | empty |
| 2 | 296 | 0.54 | 0.75 | 41 | empty |
| 3 | 239 | 0.53 | 0.76 | 41 | empty |
| 4 | 220 | 0.51 | 0.76 | 34 | empty |
| 5 | 221 | 0.49 | 0.75 | 32 | empty |
Interfaces
7 interfaces between chains.
- A–G · 829 Ų buried · 9 hydrogen bonds · protein-protein
- F–G · 827 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 822 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 820 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 811 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1G31 · GP31 co-chaperonin from bacteriophage T4 · 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 P17313
- Elsewhere: RCSB PDB 1G31 · PDBe 1G31 · UniProt P17313
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