MolNFT v1 · #146959 · protein
FE(II)-bound structure of the engineered cyt CB562 variant, CH2E
6DY4 · Soluble cytochrome B562: “FE(II)-bound structure of the engineered cyt CB562 variant, CH2E”. X-ray diffraction, 2 ligands (HEC, FE), 3 pockets (best druggability 0.71). MolNFT v1 #146959 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6DY4
- Type
- protein
- Length
- 212 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Soluble cytochrome B562
- UniProt
- P0ABE7
- Ligands
- HEC, FE
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Soluble cytochrome B562 | protein | 106 | 79% helix, 0% strand | P0ABE7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.71 | 0.98 | 18 | empty |
| 2 | 327 | 0.66 | 0.80 | 38 | HEC |
| 3 | 151 | 0.58 | 0.82 | 22 | HEC |
Interfaces
1 interface between chains.
- A–D · 691 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 cofactor, 1 disulfide (heme c attachment, disulfide).
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 P0ABE7
- Elsewhere: RCSB PDB 6DY4 · PDBe 6DY4 · UniProt P0ABE7
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