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Carbonic anhydrase CaNce103p from Candida albicans
Analyse Carbonic anhydrase CaNce103p from Candida albicans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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
- Molecule
- Carbonic anhydrase
- EC
- 4.2.1.1
- UniProt
- Q5AJ71
- Ligands
- ZN
- Pockets
- 10 · best druggability 0.79
Structure
x-ray diffraction · resolution 2.2 · 4 distinct chains · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase (EC 4.2.1.1) | protein | 208 | 49% helix, 14% strand | Q5AJ71 |
| B | Carbonic anhydrase (EC 4.2.1.1) | protein | 205 | 48% helix, 15% strand | Q5AJ71 |
| C | Carbonic anhydrase (EC 4.2.1.1) | protein | 204 | 47% helix, 15% strand | Q5AJ71 |
| D | Carbonic anhydrase (EC 4.2.1.1) | protein | 202 | 47% helix, 14% strand | 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 · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 857 | 0.79 | 0.82 | 73 | empty |
| 2 | 705 | 0.70 | 0.77 | 57 | empty |
| 3 | 371 | 0.64 | 0.79 | 33 | empty |
| 4 | 352 | 0.64 | 0.79 | 29 | empty |
| 5 | 240 | 0.51 | 0.75 | 27 | empty |
Interfaces
6 interfaces between chains.
- C–D · 3555 Ų buried · 50 hydrogen bonds · protein-protein
- A–B · 3551 Ų buried · 46 hydrogen bonds · protein-protein
- A–D · 536 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 476 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 210 Ų buried · 0 hydrogen bonds · protein-protein
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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