Research workbench
H. influenzae beta-carbonic anhydrase, variant V47A with 100 mm bicarbonate
Analyse H. influenzae beta-carbonic anhydrase, variant V47A with 100 mm bicarbonate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3E3F
- Type
- protein
- Length
- 365 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P45148
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 182 | — | P45148 |
| B | — | protein | 183 | — | P45148 |
Compared structures
- 3E3F · H. influenzae beta-carbonic anhydrase, variant V47A with 100 mM bicarbonate · the same entry in another collection · chain A against A, TM-score 1.00
- P45148 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 2 (P45148) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P45148
- Elsewhere: RCSB PDB 3E3F · PDBe 3E3F · UniProt P45148
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