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Carbonic anhydrase CAH3 from chlamydomonas reinhardtii in complex with acetazolamide
Analyse Carbonic anhydrase CAH3 from chlamydomonas reinhardtii 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
- 4XIW
- Type
- protein
- Length
- 1,903 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q39588
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | — | protein | 237 | — | Q39588 |
| C, H | — | protein | 239 | — | Q39588 |
| E, F, G | — | protein | 238 | — | Q39588 |
Compared structures
- 4XIW · Carbonic anhydrase Cah3 from Chlamydomonas reinhardtii in complex with acetazolamide · 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 Q39588
- Elsewhere: RCSB PDB 4XIW · PDBe 4XIW · UniProt Q39588
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