MolNFT v1 · #15253 · protein
Crystal structure of cytochrome C550 from thermosynechococcus elongatus
1MZ4: “Crystal structure of cytochrome C550 from thermosynechococcus elongatus”. X-ray diffraction, 3 ligands (BCT, HEC, PO4), 1 pocket (best druggability 0.70). MolNFT v1 #15253 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1MZ4
- Type
- protein
- Length
- 131 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C550
- UniProt
- P0A386
- Ligands
- BCT, HEC, PO4
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C550 | protein | 131 | 53% helix, 6% strand | P0A386 |
Ligands and binding sites
- BCT · Bicarbonate ion · ligand · chains A
- HEC · Heme C · ligand · chains A
- PO4 · Phosphate ion · ion · 5 copies · chains A
- GOL · Glycerol · additive · 5 copies · chains A
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 | 224 | 0.70 | 0.86 | 33 | 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 P0A386
- Elsewhere: RCSB PDB 1MZ4 · PDBe 1MZ4 · UniProt P0A386
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