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Crystal structure of the heme-isdc complex
Analyse Crystal structure of the heme-isdc complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O6P
- Type
- protein
- Length
- 242 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Iron-regulated surface determinant protein C
- UniProt
- Q7A654
- Ligands
- HEM, ZN, CL
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 65% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Iron-regulated surface determinant protein C | protein | 123 | 7% helix, 66% strand | Q7A654 |
| B | Iron-regulated surface determinant protein C | protein | 119 | 7% helix, 65% strand | Q7A654 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 6 copies · chains A, B
- CL · Chloride 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 | 615 | 0.74 | 0.80 | 53 | HEM |
Interfaces
1 interface between chains.
- A–B · 410 Ų buried · 1 hydrogen bond · 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 Q7A654
- Elsewhere: RCSB PDB 2O6P · PDBe 2O6P · UniProt Q7A654
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