MolNFT v1 · #127564 · protein
Crystal structure of human carbonic anhydrase II in complex with (R)- 4-(6,7-dihydroxy-1-phenyl-3,4-tetrahydroisoquinoline-1H-2-carbonyl) benzenesulfonamide.
5N0D · Carbonic anhydrase 2: “Crystal structure of human carbonic anhydrase II in complex with (R)…”. X-ray diffraction, 2 ligands (8F2, ZN), 2 pockets (best druggability 0.60). MolNFT v1 #127564 on GenesisL1: 3D structure, binding sites…
- PDB
- 5N0D
- Type
- protein
- Length
- 260 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
- 8F2, ZN
- Pockets
- 2 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 260 | 15% helix, 30% strand | P00918 |
Ligands and binding sites
- 8F2 · (R)-4-(6,7-dihydroxy-1-phenyl-3,4-tetrahydroisoquinoline-1H-2-carbonyl) benzenesulfonamide · ligand · chains A
- ZN · Zinc ion · metal · chains A
- GOL · Glycerol · additive · chains A
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 | 207 | 0.60 | 0.81 | 28 | 8F2 |
| 2 | 58 | 0.28 | 0.74 | 14 | empty |
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 5N0D · PDBe 5N0D · UniProt P00918
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