MolNFT v1 · #61469 · protein
Crystallization and structural analysis of cytochrome C6 from the diatom phaeodactylum tricornutum at 1.5 a resolution
3DMI: “Crystallization and structural analysis of cytochrome C6 from the diatom phaeodactylum tricornutum at 1.5 a…”. X-ray diffraction, 2 ligands (HEC, MG), 1 pocket (best druggability 0.71). MolNFT v1 #61469 on GenesisL1: 3D structure…
- PDB
- 3DMI
- Type
- protein
- Length
- 87 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C6
- UniProt
- Q8GTB5
- Ligands
- HEC, MG
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C6 | protein | 87 | 59% helix, 2% strand | Q8GTB5 |
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 | 202 | 0.71 | 0.88 | 32 | HEC |
Modifications
Observed in the structure: 2 cofactor (heme c attachment).
Compared structures
- 3DMI · Crystallization and Structural Analysis of Cytochrome c6 from the Diatom Phaeodactylum… · 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 Q8GTB5
- Elsewhere: RCSB PDB 3DMI · PDBe 3DMI · UniProt Q8GTB5
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