Research workbench
Crystal structure of human carbonic anhydrase II complexed with an anticonvulsant sugar sulfamate
Analyse Crystal structure of human carbonic anhydrase II complexed with an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EOU
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase II (ca II)
- EC
- 4.2.1.1
- UniProt
- P00918
- Ligands
- SMS, ZN
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase II (ca II) (EC 4.2.1.1) | protein | 258 | 15% helix, 32% strand | P00918 |
Ligands and binding sites
- SMS · Sulfamic acid 2,3-O-(1-methylethylidene)-4,5-O-sulfonyl-beta-fructopyranose ester · ligand · 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 | 135 | 0.54 | 0.81 | 25 | SMS |
Compared structures
- 1EOU · Crystal structure of human carbonic anhydrase II complexed with an anticonvulsant sugar… · the same entry in another collection · chain A against A, TM-score 1.00
- P00918 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 2 (P00918) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 1EOU · PDBe 1EOU · UniProt P00918
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