Research workbench
Fitted coordinates for groel-ATP7-groes cryo-EM complex (emd-1180)
Analyse Fitted coordinates for groel-ATP7-groes cryo-EM complex (emd-1180) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C7C
- Type
- protein
- Length
- 7,966 residues
- Chains
- 21
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 60 kda chaperonin; 10 kda chaperonin molecule: groes, protein CPN10, groes protein
- UniProt
- P0A6F5, P0A6F9
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 3 distinct chains · 48% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | 60 kda chaperonin | protein | 524 | 52% helix, 19% strand | P0A6F5 |
| H, I, J, K, L, M, N | 60 kda chaperonin | protein | 522 | 52% helix, 17% strand | P0A6F5 |
| O, P, Q, R, S, T, U | 10 kda chaperonin molecule: groes, protein CPN10, groes protein | protein | 92 | 3% helix, 38% strand | P0A6F9 |
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 | 716 | 0.83 | 0.87 | 92 | empty |
| 2 | 1043 | 0.83 | 0.84 | 110 | empty |
| 3 | 767 | 0.83 | 0.86 | 96 | empty |
| 4 | 1020 | 0.81 | 0.82 | 112 | empty |
| 5 | 477 | 0.81 | 0.88 | 68 | empty |
Interfaces
48 interfaces between chains.
- F–G · 1743 Ų buried · 25 hydrogen bonds · protein-protein
- C–D · 1711 Ų buried · 21 hydrogen bonds · protein-protein
- D–E · 1702 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 1699 Ų buried · 24 hydrogen bonds · protein-protein
- B–C · 1677 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 2C7C · Fitted coordinates for groel-ATP7-groes cryo-EM complex (emd-1180) · the same entry in another collection · chain E against E, 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 P0A6F9
- Elsewhere: RCSB PDB 2C7C · PDBe 2C7C · UniProt P0A6F5 · UniProt P0A6F9
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