Research workbench
Groel-ADP-GP31 complex
Analyse Groel-ADP-GP31 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CGT
- Type
- protein
- Length
- 7,854 residues
- Chains
- 21
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 60 kda groel; Capsid assembly protein GP31
- UniProt
- P0A6F5, P17313
- Pockets
- 20 · best druggability 0.81
Structure
electron microscopy · 3 distinct chains · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | 60 kda groel | protein | 524 | 49% helix, 18% strand | P0A6F5 |
| H, I, J, K, L, M, N | 60 kda groel | protein | 515 | 50% helix, 18% strand | P0A6F5 |
| O, P, Q, R, S, T, U | Capsid assembly protein GP31 | protein | 83 | 16% helix, 34% strand | P17313 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 330 | 0.81 | 0.91 | 52 | empty |
| 2 | 341 | 0.80 | 0.90 | 57 | empty |
| 3 | 380 | 0.80 | 0.89 | 58 | empty |
| 4 | 348 | 0.80 | 0.89 | 58 | empty |
| 5 | 351 | 0.79 | 0.89 | 58 | empty |
Interfaces
42 interfaces between chains.
- A–B · 1733 Ų buried · 21 hydrogen bonds · protein-protein
- C–D · 1732 Ų buried · 21 hydrogen bonds · protein-protein
- D–E · 1730 Ų buried · 21 hydrogen bonds · protein-protein
- A–G · 1729 Ų buried · 21 hydrogen bonds · protein-protein
- B–C · 1729 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 2CGT · GROEL-ADP-gp31 COMPLEX · the same entry in another collection · chain K against K, 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 P0A6F5
- Every structure of UniProt P17313
- Elsewhere: RCSB PDB 2CGT · PDBe 2CGT · UniProt P0A6F5 · UniProt P17313
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