Research workbench
Human Carbonic Anhydrase II in complex with 4-(3-(3-phenoxypropyl)thioureido)benzenesulfonamide
Analyse Human Carbonic Anhydrase II in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7A6V
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Homo sapiens
- Molecule
- Carbonic anhydrase 2
- EC
- 4.2.1.1
- UniProt
- P00918
- Ligands
- R2W, ZN
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 16% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase 2 (EC 4.2.1.1) | protein | 258 | 16% helix, 31% strand | P00918 |
Ligands and binding sites
- R2W · 4-(3-(3-phenoxypropyl)thioureido)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
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 | 154 | 0.57 | 0.82 | 27 | GOL, R2W |
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 7A6V · PDBe 7A6V · UniProt P00918
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