MolNFT v1 · #31077 · protein
Crystal structure of mouse testicular cytochrome C at 1.6 ångström
2AIU · Cytochrome C, testis-specific: “Crystal structure of mouse testicular cytochrome C at 1.6 ångström”. X-ray diffraction, 2 ligands (HEM, PO4), 1 pocket (best druggability 0.76). MolNFT v1 #31077 on GenesisL1: 3D structure, binding…
- PDB
- 2AIU
- Type
- protein
- Length
- 104 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C, testis-specific
- UniProt
- P00015
- Ligands
- HEM, PO4
- Pockets
- 1 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C, testis-specific | protein | 104 | 43% helix, 2% strand | P00015 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- PO4 · Phosphate ion · ion · 2 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 | 184 | 0.76 | 0.92 | 34 | HEM |
Modifications
Observed in the structure: 2 cofactor (heme attachment).
Compared structures
- 2AIU · Crystal Structure of Mouse Testicular Cytochrome C at 1.6 Angstrom · the same entry in another collection · chain A against A, TM-score 1.00
- P00015 · AlphaFold monomer V2.0 prediction for cytochrome C, testis-specific (P00015) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P00015
- Elsewhere: RCSB PDB 2AIU · PDBe 2AIU · UniProt P00015
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