Research workbench
Crystal structure of Ca_00311
Analyse Crystal structure of Ca_00311 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BXB
- Type
- protein
- Length
- 1,320 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.72
- Source
- Collinsella aerofaciens
- Molecule
- GDSL-like Lipase/Acylhydrolase
- UniProt
- A0A381K2L8
- Ligands
- PO4
- Pockets
- 13 · best druggability 0.85
Structure
x-ray diffraction · resolution 1.72 · 1 distinct chain · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | GDSL-like Lipase/Acylhydrolase | protein | 220 | 45% helix, 16% strand | A0A381K2L8 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 15 copies · chains A, F, B, E, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 491 | 0.85 | 0.91 | 60 | PO4 |
| 2 | 509 | 0.84 | 0.91 | 58 | PO4 |
| 3 | 308 | 0.79 | 0.89 | 31 | empty |
| 4 | 286 | 0.77 | 0.89 | 33 | empty |
| 5 | 248 | 0.76 | 0.89 | 30 | empty |
Interfaces
15 interfaces between chains.
- B–E · 1219 Ų buried · 9 hydrogen bonds · protein-protein
- A–F · 1206 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 1191 Ų buried · 10 hydrogen bonds · protein-protein
- E–F · 651 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 648 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 7BXB · Crystal structure of CA_00311 · 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 A0A381K2L8
- Elsewhere: RCSB PDB 7BXB · PDBe 7BXB · UniProt A0A381K2L8
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