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Crystal structures of two tetrameric beta-carbonic anhydrases from the filamentous ascomycete sordaria macrospora.
Analyse Crystal structures of two tetrameric beta-carbonic anhydrases from the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4O1K
- Type
- protein
- Length
- 211 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbonic anhydrase
- EC
- 4.2.1.1
- UniProt
- C1L336
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbonic anhydrase (EC 4.2.1.1) | protein | 211 | 52% helix, 15% strand | C1L336 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4O1K · Crystal structures of two tetrameric beta-carbonic anhydrases from the filamentous… · the same entry in another collection · 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 C1L336
- Elsewhere: RCSB PDB 4O1K · PDBe 4O1K · UniProt C1L336
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