Research workbench
Human carbonic anhydrase in complex with CO2
Analyse Human carbonic anhydrase in complex with CO2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VVA
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase 2
- EC
- 4.2.1.1
- UniProt
- P00918
- Ligands
- ZN, CO2, SO4
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 258 | 16% helix, 31% strand | P00918 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains X
- CO2 · Carbon dioxide · ion · 2 copies · chains X
- SO4 · Sulfate ion · ion · chains X
- GOL · Glycerol · additive · 2 copies · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 131 | 0.55 | 0.82 | 24 | SO4, CO2 |
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 P00918
- Elsewhere: RCSB PDB 2VVA · PDBe 2VVA · UniProt P00918
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