Research workbench
Site-specific mutant (HIS64 replaced with ala) of human carbonic anhydrase II complexed with 4-methylimidazole
Analyse Site-specific mutant (HIS64 replaced with ala) of human carbonic anhydrase II… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G0E
- Type
- protein
- Length
- 258 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
- 4MZ, ZN, HG
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase II (EC 4.2.1.1) | protein | 258 | 15% helix, 31% strand | P00918 |
Ligands and binding sites
- 4MZ · 4-methylimidazole · ligand · chains A
- ZN · Zinc ion · metal · chains A
- HG · Mercury (II) 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 | 140 | 0.56 | 0.82 | 24 | empty |
Compared structures
- 1G0E · Site-specific mutant (HIS64 replaced with ala) of human carbonic anhydrase II complexed… · 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 1G0E · PDBe 1G0E · UniProt P00918
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