Research workbench
Structure of fungal alpha carbonic anhydrase from aspergillus oryzae
Analyse Structure of fungal alpha carbonic anhydrase from aspergillus oryzae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3Q31
- Type
- protein
- Length
- 472 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase
- EC
- 4.2.1.1
- UniProt
- Q2TWF5
- Ligands
- MLT, NAG, ZN
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Carbonic anhydrase (EC 4.2.1.1) | protein | 236 | 21% helix, 32% strand | Q2TWF5 |
Ligands and binding sites
- MLT · D-malate · ligand · 2 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.76 | 0.97 | 35 | empty |
| 2 | 135 | 0.51 | 0.79 | 25 | MLT |
| 3 | 110 | 0.46 | 0.79 | 25 | MLT |
| 4 | 66 | 0.31 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1937 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 3Q31 · Structure of fungal alpha Carbonic Anhydrase from Aspergillus oryzae · 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 Q2TWF5
- Elsewhere: RCSB PDB 3Q31 · PDBe 3Q31 · UniProt Q2TWF5
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