Research workbench
Reduced structure of cytochrome C3 from desulfovibrio desulfuricans atcc 27774 at pH 7.6
Analyse Reduced structure of cytochrome C3 from desulfovibrio desulfuricans atcc 27774… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UP9
- Type
- protein
- Length
- 107 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C3
- UniProt
- Q9L915
- Ligands
- HEC, SO4
- Pockets
- 1 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C3 | protein | 107 | 30% helix, 11% strand | Q9L915 |
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 | 755 | 0.77 | 0.81 | 75 | HEC |
Modifications
Observed in the structure: 8 cofactor (heme c attachment).
Compared structures
- 1UP9 · Reduced structure of cytochrome C3 from desulfovibrio desulfuricans atcc 27774 at pH 7.6 · 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 Q9L915
- Elsewhere: RCSB PDB 1UP9 · PDBe 1UP9 · UniProt Q9L915
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