Research workbench
Crystal structure of the Y200A mutant of gamma carbonic anhydrase from methanosarcina thermophila
Analyse Crystal structure of the Y200A mutant of gamma carbonic anhydrase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OW5
- Type
- protein
- Length
- 205 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase
- EC
- 4.2.1.1
- UniProt
- P40881
- Ligands
- BCT, ZN, FE, SO4
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase (EC 4.2.1.1) | protein | 205 | 12% helix, 36% strand | P40881 |
Ligands and binding sites
- BCT · Bicarbonate ion · ligand · chains A
- ZN · Zinc ion · metal · chains A
- FE · Fe (III) ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3OW5 · Crystal structure of the Y200A mutant of gamma carbonic anhydrase from Methanosarcina… · the same entry in another collection · chain A against A, TM-score 1.00
- P40881 · AlphaFold monomer V2.0 prediction for carbonic anhydrase (P40881) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P40881
- Elsewhere: RCSB PDB 3OW5 · PDBe 3OW5 · UniProt P40881
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