MolNFT v1 · #14203 · protein
Reduced P222 crystal structure of the tetraheme cytochrome C of shewanella oneidensis MR1
1M1R · Small tetraheme cytochrome C: “Reduced P222 crystal structure of the tetraheme cytochrome C of shewanella oneidensis MR1”. X-ray diffraction, 2 ligands (HEC, SO4), 1 pocket (best druggability 0.68). MolNFT v1 #14203 on GenesisL1: 3D…
- PDB
- 1M1R
- Type
- protein
- Length
- 91 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Small tetraheme cytochrome C
- UniProt
- Q8EDL6
- Ligands
- HEC, SO4
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Small tetraheme cytochrome C | protein | 91 | 41% helix, 2% strand | Q8EDL6 |
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 | 402 | 0.68 | 0.80 | 55 | HEC |
Modifications
Observed in the structure: 8 cofactor (heme c attachment).
Compared structures
- 1M1R · Reduced p222 crystal structure of the tetraheme cytochrome c of Shewanella oneidensis MR1 · 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 Q8EDL6
- Elsewhere: RCSB PDB 1M1R · PDBe 1M1R · UniProt Q8EDL6
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