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The crystal structure of an alpha carbonic anhydrase from the extremophilic bacterium sulfurihydrogenibium azorense.
Analyse The crystal structure of an alpha carbonic anhydrase from the extremophilic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4X5S
- Type
- protein
- Length
- 446 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase (carbonate dehydratase)
- EC
- 4.2.1.1
- UniProt
- C1DTU5
- Ligands
- AZM, ZN
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Carbonic anhydrase (carbonate dehydratase) (EC 4.2.1.1) | protein | 223 | 17% helix, 35% strand | C1DTU5 |
Ligands and binding sites
- AZM · 5-acetamido-1,3,4-thiadiazole-2-sulfonamide · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
- PE8 · 3,6,9,12,15,18,21-heptaoxatricosane-1,23-diol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 161 | 0.50 | 0.78 | 24 | AZM |
| 2 | 153 | 0.47 | 0.77 | 24 | AZM |
Interfaces
1 interface between chains.
- A–B · 1077 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4X5S · The crystal structure of an alpha carbonic anhydrase from the extremophilic bacterium… · 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 C1DTU5
- Elsewhere: RCSB PDB 4X5S · PDBe 4X5S · UniProt C1DTU5
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