Research workbench
Human Heme Oxygenase Oxidatition of alpha- and gamma-meso-Phenylhemes
Analyse Human Heme Oxygenase Oxidatition of alpha- and gamma-meso-Phenylhemes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1S13
- Type
- protein
- Length
- 428 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.29
- Source
- Homo sapiens
- Molecule
- Heme oxygenase 1
- EC
- 1.14.99.3
- UniProt
- P09601
- Ligands
- 2FH
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · resolution 2.29 · 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
- 2FH · 2-phenylheme · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 394 | 0.76 | 0.85 | 38 | 2FH |
| 2 | 397 | 0.74 | 0.84 | 40 | 2FH |
| 3 | 51 | 0.45 | 0.84 | 17 | empty |
| 4 | 50 | 0.45 | 0.84 | 13 | empty |
Compared structures
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 1S13 · PDBe 1S13 · UniProt P09601
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.