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The active site base controls cofactor reactivity in escherichia COLI amine oxidase : X-ray crystallographic studies with mutational variants
Analyse The active site base controls cofactor reactivity in escherichia COLI amine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QAF
- Type
- protein
- Length
- 1,439 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P46883
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 718 | — | P46883 |
| B | — | protein | 721 | — | P46883 |
Compared structures
- 1QAF · The active site base controls cofactor reactivity in escherichia COLI amine oxidase… · the same entry in another collection · chain A against A, TM-score 1.00
- P46883 · AlphaFold monomer V2.0 prediction for primary amine oxidase (P46883) · 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 P46883
- Elsewhere: RCSB PDB 1QAF · PDBe 1QAF · UniProt P46883
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