Research workbench
Structure of the chaperonin GP146 from the bacteriophage el (pseudomonas aeruginosa) in the apo state
Analyse Structure of the chaperonin GP146 from the bacteriophage el (pseudomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TMV
- Type
- protein
- Length
- 7,604 residues
- Chains
- 14
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative groel-like chaperonine protein
- UniProt
- Q2Z0T5
- Pockets
- 20 · best druggability 0.80
Structure
electron microscopy · 2 distinct chains · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, H, J, L | Putative groel-like chaperonine protein | protein | 546 | 49% helix, 15% strand | Q2Z0T5 |
| B, D, F, G, I, K, M, N | Putative groel-like chaperonine protein | protein | 541 | 49% helix, 16% strand | Q2Z0T5 |
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 | 959 | 0.80 | 0.82 | 91 | empty |
| 2 | 838 | 0.80 | 0.83 | 81 | empty |
| 3 | 1013 | 0.79 | 0.81 | 79 | empty |
| 4 | 930 | 0.79 | 0.81 | 78 | empty |
| 5 | 1127 | 0.79 | 0.80 | 97 | empty |
Interfaces
28 interfaces between chains.
- E–F · 1492 Ų buried · 13 hydrogen bonds · protein-protein
- L–M · 1482 Ų buried · 13 hydrogen bonds · protein-protein
- H–I · 1465 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 1458 Ų buried · 13 hydrogen bonds · protein-protein
- J–K · 1437 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 6TMV · Structure of the chaperonin gp146 from the bacteriophage EL (Pseudomonas aeruginosa) in… · 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 Q2Z0T5
- Elsewhere: RCSB PDB 6TMV · PDBe 6TMV · UniProt Q2Z0T5
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