Research workbench
Crystal structure of protein VC1899 from vibrio cholerae
Analyse Crystal structure of protein VC1899 from vibrio cholerae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XMX
- Type
- protein
- Length
- 380 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein VC1899
- UniProt
- Q9KQU9
- Ligands
- MG
- Pockets
- 3 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein VC1899 | protein | 380 | 48% helix, 24% strand | Q9KQU9 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
- FMT · Formic acid · additive · 6 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 167 | 0.47 | 0.76 | 28 | empty |
| 2 | 68 | 0.42 | 0.81 | 16 | GOL |
| 3 | 83 | 0.34 | 0.74 | 16 | FMT |
Compared structures
- 1XMX · Crystal structure of protein VC1899 from Vibrio cholerae · 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 Q9KQU9
- Elsewhere: RCSB PDB 1XMX · PDBe 1XMX · UniProt Q9KQU9
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