MolNFT v1 · #98859 · protein
Crystal structure of the outer membrane decaheme cytochrome mtrc
4LM8 · Extracellular iron oxide respiratory system surface…: “Crystal structure of the outer membrane decaheme cytochrome mtrc”. X-ray diffraction, 2 ligands (HEC, CA), 7 pockets (best druggability 0.86). MolNFT v1 #98859 on GenesisL1: 3D…
- PDB
- 4LM8
- Type
- protein
- Length
- 626 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Extracellular iron oxide respiratory system surface decaheme cytochrome C component mtrc
- UniProt
- Q8EG34
- Ligands
- HEC, CA
- Pockets
- 7 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Extracellular iron oxide respiratory system surface decaheme cytochrome C component mtrc | protein | 626 | 23% helix, 25% strand | Q8EG34 |
Ligands and binding sites
- HEC · Heme C · ligand · 10 copies · chains A
- CA · Calcium ion · metal · 5 copies · chains A
- EDO · 1,2-ethanediol · additive · 8 copies · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 561 | 0.86 | 0.91 | 75 | HEC |
| 2 | 526 | 0.85 | 0.91 | 61 | HEC, EDO |
| 3 | 74 | 0.63 | 0.90 | 19 | HEC |
| 4 | 120 | 0.50 | 0.80 | 16 | EDO |
| 5 | 65 | 0.36 | 0.78 | 22 | empty |
Modifications
Observed in the structure: 19 cofactor, 1 disulfide (heme c attachment, disulfide).
Compared structures
- 4LM8 · Crystal structure of the outer membrane decaheme cytochrome MtrC · 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 Q8EG34
- Elsewhere: RCSB PDB 4LM8 · PDBe 4LM8 · UniProt Q8EG34
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