Research workbench
CO(II)-bound structure of the engineered cyt CB562 variant, H3
Analyse CO(II)-bound structure of the engineered cyt CB562 variant, H3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DYI
- Type
- protein
- Length
- 106 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Soluble cytochrome B562
- UniProt
- P0ABE7
- Ligands
- HEC, CA, CO, CL
- Pockets
- 1 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Soluble cytochrome B562 | protein | 106 | 76% helix, 0% strand | P0ABE7 |
Ligands and binding sites
- HEC · Heme C · ligand · chains B
- CA · Calcium ion · metal · 6 copies · chains B
- CO · Cobalt (II) ion · metal · chains B
- CL · Chloride ion · ion · chains 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 | 192 | 0.59 | 0.81 | 28 | HEC |
Modifications
Observed in the structure: 2 cofactor (heme c attachment).
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 6DYI · PDBe 6DYI · UniProt P0ABE7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.