MolNFT v1 · #37052 · protein
Human carbonic anhydrase II complexed with two-prong inhibitors
2FOS: “Human carbonic anhydrase II complexed with two-prong inhibitors”. X-ray diffraction, 3 ligands (B17, CU, ZN), 1 pocket (best druggability 0.58). MolNFT v1 #37052 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2FOS
- Type
- protein
- Length
- 259 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase II
- EC
- 4.2.1.1
- UniProt
- P00918
- Ligands
- B17, CU, ZN
- Pockets
- 1 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase II (EC 4.2.1.1) | protein | 259 | 15% helix, 30% strand | P00918 |
Ligands and binding sites
- B17 · {1-[4-(aminosulfonyl)phenyl]-11-[(carboxy-kappao)methyl]-1-oxo-5,8-dioxa-2,11-diazatridecan-13-oato(2-)-kappao~13~}copper · ligand · 2 copies · chains A
- CU · Copper (II) ion · metal · 2 copies · chains A
- ZN · Zinc ion · metal · chains A
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 | 180 | 0.58 | 0.81 | 26 | B17 |
Modifications
Observed in the structure: 1 modified (nonstandard).
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 2FOS · PDBe 2FOS · UniProt P00918
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