Research workbench
Crystal structures of the ferric, ferrous, and ferrous-no forms of the ASP140ALA mutant of human heme oxygenase-1: catalytic implications
Analyse Crystal structures of the ferric, ferrous, and ferrous-no forms of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OYK
- Type
- protein
- Length
- 428 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P09601
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 214 | — | P09601 |
Compared structures
- 1OYK · Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant… · the same entry in another collection · chain A against A, TM-score 1.00
- P09601 · AlphaFold monomer V2.0 prediction for heme oxygenase 1 (P09601) · a predicted model of the same protein · chain A 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 P09601
- Elsewhere: RCSB PDB 1OYK · PDBe 1OYK · UniProt P09601
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