Research workbench
The X-ray structure of heme-bound murine HEBP1
Analyse The X-ray structure of heme-bound murine HEBP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OON
- Type
- protein
- Length
- 369 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heme-binding protein 1
- UniProt
- Q9R257
- Ligands
- HEM, SO4
- Pockets
- 1 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heme-binding protein 1 | protein | 184 | 18% helix, 41% strand | Q9R257 |
| B | Heme-binding protein 1 | protein | 185 | 19% helix, 40% strand | Q9R257 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
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 | 1139 | 0.79 | 0.80 | 72 | HEM |
Interfaces
1 interface between chains.
- A–B · 872 Ų buried · 2 hydrogen bonds · protein-protein
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 Q9R257
- Elsewhere: RCSB PDB 7OON · PDBe 7OON · UniProt Q9R257
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