Research workbench
NMR solution structures of fully oxidised cytochrome C3 from desulfovibrio desulfuricans atcc 27774
Analyse NMR solution structures of fully oxidised cytochrome C3 from desulfovibrio… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KMY
- Type
- protein
- Length
- 107 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C3
- UniProt
- Q9L915
- Ligands
- HEC
- Pockets
- 1 · best druggability 0.75
Structure
solution nmr · 1 distinct chain · 15% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C3 | protein | 107 | 15% helix, 7% strand | Q9L915 |
Ligands and binding sites
- HEC · Heme C · ligand · 4 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 | 845 | 0.75 | 0.79 | 71 | HEC |
Modifications
Observed in the structure: 8 cofactor (heme c attachment).
Compared structures
- 2KMY · NMR Solution structures of fully oxidised cytochrome c3 from Desulfovibrio desulfuricans… · 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 2KMY · PDBe 2KMY · UniProt Q9L915
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