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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
- 1OZE
- Type
- protein
- Length
- 428 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heme oxygenase 1
- EC
- 1.14.99.3
- UniProt
- P09601
- Ligands
- HEM
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Heme oxygenase 1 (EC 1.14.99.3) | protein | 214 | 76% helix, 0% strand | P09601 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 440 | 0.79 | 0.86 | 39 | HEM |
| 2 | 418 | 0.78 | 0.86 | 38 | HEM |
| 3 | 294 | 0.63 | 0.80 | 35 | empty |
| 4 | 99 | 0.44 | 0.79 | 19 | empty |
| 5 | 104 | 0.38 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1151 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 1OZE · 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 1OZE · PDBe 1OZE · UniProt P09601
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