Research workbench
S-class cytochromes C have a variety of folding patterns: structure of cytochrome C-553 from desulfovibrio vulgaris determined by the multi-wavelength anomalous dispersion method
Analyse S-class cytochromes C have a variety of folding patterns: structure of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1C53
- Type
- protein
- Length
- 79 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C553
- UniProt
- P00120
- Ligands
- HEM
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C553 | protein | 79 | 0% helix, 0% strand | P00120 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1C53 · S-class cytochromes C have a variety of folding patterns: structure of cytochrome C-553… · the same entry in another collection · chain A against A, TM-score 1.00
- P00120 · AlphaFold monomer V2.0 prediction for cytochrome C-553 (P00120) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P00120
- Elsewhere: RCSB PDB 1C53 · PDBe 1C53 · UniProt P00120
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