Research workbench
Comparisions of the heme-free and-bound crystal structures of human heme oxygenase-1
Analyse Comparisions of the heme-free and-bound crystal structures of human heme… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NI6
- Type
- protein
- Length
- 865 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P09601
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 215 | — | P09601 |
| B | — | protein | 214 | — | P09601 |
| C | — | protein | 223 | — | P09601 |
| D | — | protein | 213 | — | P09601 |
Compared structures
- 1NI6 · Comparisions of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1 · the same entry in another collection · chain D against D, 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 1NI6 · PDBe 1NI6 · UniProt P09601
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