MolNFT v1 · #2944 · protein
The asp-his-fe triad of cytochrome C peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free- radical to the heme
1CCB: “The asp-his-fe triad of cytochrome C peroxidase controls the reduction potential, electronic structure, and…”. X-ray diffraction. MolNFT v1 #2944 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1CCB
- Type
- protein
- Length
- 291 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00431
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 291 | — | P00431 |
Compared structures
- 1CCB · The asp-his-fe triad of cytochrome C peroxidase controls the reduction potential… · the same entry in another collection · chain A against A, TM-score 1.00
- P00431 · AlphaFold monomer V2.0 prediction for cytochrome C peroxidase, mitochondrial (P00431) · a predicted model of the same protein · 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 P00431
- Elsewhere: RCSB PDB 1CCB · PDBe 1CCB · UniProt P00431
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