Research workbench
Oxidase chap-D49L/Y109F mutant
Analyse Oxidase chap-D49L/Y109F mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7WB2
- Type
- protein
- Length
- 477 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q4R0L3
- Ligands
- FE
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 118 | — | Q4R0L3 |
| B | — | protein | 120 | — | Q4R0L3 |
| C | — | protein | 119 | — | Q4R0L3 |
| D | — | protein | 120 | — | Q4R0L3 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 15 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7WB2 · Oxidase ChaP-D49L/Y109F mutant · 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 Q4R0L3
- Elsewhere: RCSB PDB 7WB2 · PDBe 7WB2 · UniProt Q4R0L3
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