Research workbench
The Y64A mutant of cytochrome C553 from desulfovibrio vulgaris hildenborough, NMR, 39 structures
Analyse The Y64A mutant of cytochrome C553 from desulfovibrio vulgaris hildenborough… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DVH
- Type
- protein
- Length
- 79 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C-553
- UniProt
- P04032
- Ligands
- HEC
- Pockets
- 1 · best druggability 0.69
Structure
solution nmr · 1 distinct chain · 56% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C-553 | protein | 79 | 56% helix, 0% strand | P04032 |
Ligands and binding sites
- HEC · Heme C · ligand · 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 | 231 | 0.69 | 0.85 | 26 | HEC |
Modifications
Observed in the structure: 2 cofactor (heme c attachment).
Compared structures
- 2DVH · The Y64A mutant of cytochrome C553 from desulfovibrio vulgaris hildenborough, NMR, 39… · the same entry in another collection · chain A against A, TM-score 1.00
- P04032 · AlphaFold monomer V2.0 prediction for cytochrome C-553 (P04032) · a predicted model of the same protein · chain A against A, TM-score 0.86
- 1DWL · The Ferredoxin-Cytochrome complex using heteronuclear NMR and docking simulation · a predicted model of the same protein · chain A against B, TM-score 0.66
- 1DWL · The ferredoxin-cytochrome complex using heteronuclear NMR and docking simulation · a predicted model of the same protein · chain A against B, TM-score 0.66
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 P04032
- Elsewhere: RCSB PDB 2DVH · PDBe 2DVH · UniProt P04032
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