Research workbench
Rat heme oxygenase-1 in complex with heme and co at 100 K after warming to 160 K
Analyse Rat heme oxygenase-1 in complex with heme and co at 100 K after warming to 160 K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4G99
- Type
- protein
- Length
- 212 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heme oxygenase 1
- EC
- 1.14.99.3
- UniProt
- P06762
- Ligands
- HEM, CMO
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heme oxygenase 1 (EC 1.14.99.3) | protein | 212 | 75% helix, 0% strand | P06762 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- CMO · Carbon monoxide · ion · chains A
- FMT · Formic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 329 | 0.74 | 0.85 | 34 | HEM, CMO |
Compared structures
- 4G99 · Rat Heme Oxygenase-1 in complex with Heme and CO at 100 K after warming to 160 K · the same entry in another collection · chain A against A, TM-score 1.00
- P06762 · AlphaFold monomer V2.0 prediction for heme oxygenase 1 (P06762) · a predicted model of the same protein · 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 P06762
- Elsewhere: RCSB PDB 4G99 · PDBe 4G99 · UniProt P06762
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