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Structure of the FE3+-biliverdin-hmuo, heme oxygenase from corynebacterium diphtheriae (data set III)
Analyse Structure of the FE3+-biliverdin-hmuo, heme oxygenase from corynebacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GPF
- Type
- protein
- Length
- 624 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q54AI1
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 207 | — | Q54AI1 |
| B | — | protein | 209 | — | Q54AI1 |
| C | — | protein | 208 | — | Q54AI1 |
Compared structures
- 4GPF · Structure of the Fe3+-biliverdin-HmuO, heme oxygenase from Corynebacterium diphtheriae… · 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 Q54AI1
- Elsewhere: RCSB PDB 4GPF · PDBe 4GPF · UniProt Q54AI1
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