Research workbench
Structure of rice ferricytochrome C at 2.0 ångströms resolution
Analyse Structure of rice ferricytochrome C at 2.0 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CCR
- Type
- protein
- Length
- 111 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C
- UniProt
- P00055
- Ligands
- ACE, HEC
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C | protein | 111 | 42% helix, 2% strand | P00055 |
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 | 199 | 0.75 | 0.90 | 35 | HEC |
Modifications
Observed in the structure: 2 cofactor, 2 modified, 1 covalent (heme c attachment, methylation, covalent ligand).
Compared structures
- 1CCR · Structure of rice ferricytochrome C at 2.0 ångströms resolution · 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 P00055
- Elsewhere: RCSB PDB 1CCR · PDBe 1CCR · UniProt P00055
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