MolNFT v1 · #145660 · protein
Engineered cytochrome C from rhodothermus marinus (rma tde) bound to carbene intermediate (1-ethoxy-1-oxopropan-2-ylidene)
6CUN: “Engineered cytochrome C from rhodothermus marinus (rma tde) bound to carbene intermediate…”. X-ray diffraction, 2 ligands (HEC, CA1), 1 pocket (best druggability 0.70). MolNFT v1 #145660 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6CUN
- Type
- protein
- Length
- 112 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C
- UniProt
- B3FQS5
- Ligands
- HEC, CA1
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C | protein | 112 | 63% helix, 0% strand | B3FQS5 |
Ligands and binding sites
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 | 420 | 0.70 | 0.81 | 32 | HEC, CA1 |
Modifications
Observed in the structure: 2 cofactor (heme c attachment).
Compared structures
- 6CUN · Engineered Cytochrome c from Rhodothermus marinus (Rma TDE) bound to carbene intermediate… · the same entry in another collection · chain A against A, TM-score 1.00
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 B3FQS5
- Elsewhere: RCSB PDB 6CUN · PDBe 6CUN · UniProt B3FQS5
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