MolNFT v2 · #151497 · protein
Carbonic anhydrase CaNce103p from Candida albicans
6GWU: “Carbonic anhydrase CaNce103p from Candida albicans”. X-ray diffraction at 2.2, 1 ligand (ZN). MolNFT v2 #151497 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6GWU
- Type
- protein
- Length
- 819 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.2
- Source
- Candida albicans
- UniProt
- Q5AJ71
- Ligands
- ZN
Structure
x-ray diffraction · resolution 2.2 · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 208 | — | Q5AJ71 |
| B | — | protein | 205 | — | Q5AJ71 |
| C | — | protein | 204 | — | Q5AJ71 |
| D | — | protein | 202 | — | Q5AJ71 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
- BME · Beta-mercaptoethanol · additive · 4 copies · chains A, B, C, D
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B
- PGE · Triethylene glycol · additive
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 Q5AJ71
- Elsewhere: RCSB PDB 6GWU · PDBe 6GWU · UniProt Q5AJ71
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