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Crystal structure of protein VC1974 from vibrio cholerae, pfam abhydrolase
Analyse Crystal structure of protein VC1974 from vibrio cholerae, pfam abhydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1R3D
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Conserved hypothetical protein VC1974
- UniProt
- Q9KQM4
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Conserved hypothetical protein VC1974 | protein | 257 | 48% helix, 16% strand | Q9KQM4 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 206 | 0.76 | 0.91 | 33 | empty |
| 2 | 69 | 0.40 | 0.79 | 15 | empty |
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 1R3D · Crystal structure of protein VC1974 from Vibrio cholerae, Pfam abhydrolase · 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 Q9KQM4
- Elsewhere: RCSB PDB 1R3D · PDBe 1R3D · UniProt Q9KQM4
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