Research workbench
Crystal structure of ripc from yersinia pestis
Analyse Crystal structure of ripc from yersinia pestis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QLL
- Type
- protein
- Length
- 645 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Citrate lyase
- UniProt
- Q9ZC38
- Pockets
- 6 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Citrate lyase | protein | 215 | 47% helix, 18% strand | Q9ZC38 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 222 | 0.66 | 0.84 | 27 | empty |
| 2 | 187 | 0.66 | 0.85 | 34 | empty |
| 3 | 179 | 0.51 | 0.78 | 24 | empty |
| 4 | 171 | 0.47 | 0.76 | 28 | empty |
| 5 | 147 | 0.45 | 0.76 | 28 | empty |
Interfaces
3 interfaces between chains.
- A–B · 514 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 465 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 464 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 3QLL · Crystal Structure of RipC from Yersinia pestis · 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 Q9ZC38
- Elsewhere: RCSB PDB 3QLL · PDBe 3QLL · UniProt Q9ZC38
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