Research workbench
The crystal structure of the bacterial chaperonin groel at 2.8 ångströms
Analyse The crystal structure of the bacterial chaperonin groel at 2.8 ångströms in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GRL
- Type
- protein
- Length
- 3,626 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Groel (HSP60 class)
- UniProt
- P06139
- Pockets
- 20 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Groel (HSP60 class) | protein | 518 | 46% helix, 11% strand | P06139 |
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 843 | 0.75 | 0.79 | 85 | empty |
| 2 | 1130 | 0.74 | 0.77 | 100 | empty |
| 3 | 748 | 0.74 | 0.79 | 82 | empty |
| 4 | 1102 | 0.73 | 0.77 | 93 | empty |
| 5 | 1105 | 0.73 | 0.77 | 102 | empty |
Interfaces
7 interfaces between chains.
- E–F · 1273 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1270 Ų buried · 18 hydrogen bonds · protein-protein
- D–E · 1269 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1188 Ų buried · 13 hydrogen bonds · protein-protein
- A–G · 1185 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 1GRL · The crystal structure of the bacterial chaperonin groel at 2.8 ångströms · 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 P06139
- Elsewhere: RCSB PDB 1GRL · PDBe 1GRL · UniProt P06139
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