MolNFT v1 · #115126 · protein
Refined structure of human carbonic anhydrase II at 2.0 ångströms resolution
5CAC · Carbonic anhydrase form C: “Refined structure of human carbonic anhydrase II at 2.0 ångströms resolution”. X-ray diffraction, 2 ligands (ZN, SO3), 1 pocket (best druggability 0.55). MolNFT v1 #115126 on GenesisL1: 3D structure…
- PDB
- 5CAC
- Type
- protein
- Length
- 256 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase form C
- EC
- 4.2.1.1
- UniProt
- P00918
- Ligands
- ZN, SO3
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase form C (EC 4.2.1.1) | protein | 256 | 15% helix, 30% strand | P00918 |
Ligands and binding sites
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 | 121 | 0.55 | 0.83 | 26 | SO3 |
Compared structures
- P00918 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 2 (P00918) · a predicted model of the same protein · 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 P00918
- Elsewhere: RCSB PDB 5CAC · PDBe 5CAC · UniProt P00918
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