MolNFT v1 · #9489 · protein
Crystal structure of the catalytic domain of yope-yersinia pestis gap effector protein.
1HY5 · Yersinia pestis virulence protein yope: “Crystal structure of the catalytic domain of yope-yersinia pestis gap effector protein.”. X-ray diffraction. MolNFT v1 #9489 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1HY5
- Type
- protein
- Length
- 241 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Yersinia pestis virulence protein yope
- UniProt
- P31493
Structure
x-ray diffraction · 2 distinct chains · 73% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Yersinia pestis virulence protein yope | protein | 120 | 73% helix, 3% strand | P31493 |
| B | Yersinia pestis virulence protein yope | protein | 121 | 72% helix, 3% strand | P31493 |
Interfaces
1 interface between chains.
- A–B · 348 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 1HY5 · Crystal structure of the catalytic domain of yope-yersinia pestis gap effector protein. · the same entry in another collection · chain A against A, TM-score 1.00
- P31493 · AlphaFold monomer V2.0 prediction for outer membrane virulence protein yope (P31493) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P31493
- Elsewhere: RCSB PDB 1HY5 · PDBe 1HY5 · UniProt P31493
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