MolNFT v1 · #45466 · protein
NMR structure of the Y48PCMF variant of human cytochrome C in its reduced state
2N3Y: “NMR structure of the Y48PCMF variant of human cytochrome C in its reduced state”. Solution nmr, 1 ligand (MH0), 1 pocket (best druggability 0.73). MolNFT v1 #45466 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2N3Y
- Type
- protein
- Length
- 104 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C
- UniProt
- P99999
- Ligands
- MH0
- Pockets
- 1 · best druggability 0.73
Structure
solution nmr · 1 distinct chain · 38% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C | protein | 104 | 38% helix, 0% strand | P99999 |
Ligands and binding sites
- MH0 · Mesoheme · 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 | 307 | 0.73 | 0.85 | 42 | MH0 |
Modifications
Observed in the structure: 2 covalent, 1 modified (covalent ligand, nonstandard).
Compared structures
- 2N3Y · NMR structure of the Y48pCMF variant of human cytochrome c in its reduced state · the same entry in another collection · chain A against A, TM-score 1.00
- P99999 · AlphaFold monomer V2.0 prediction for cytochrome C (P99999) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 P99999
- Elsewhere: RCSB PDB 2N3Y · PDBe 2N3Y · UniProt P99999
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.