MolNFT v1 · #21150 · protein
Human heme oxygenase oxidatition of alpha- and gamma-meso- phenylhemes
1S13 · Heme oxygenase 1: “Human heme oxygenase oxidatition of alpha- and gamma-meso- phenylhemes”. X-ray diffraction, 1 ligand (2FH), 4 pockets (best druggability 0.76). MolNFT v1 #21150 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1S13
- 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
- 2FH
- Pockets
- 4 · best druggability 0.76
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
- 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
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