MolNFT v1 · #4444 · protein
Solution structure of oxidized microsomal rabbit cytochrome B5. factors determining the heterogeneous binding of the heme.
1DO9: “Solution structure of oxidized microsomal rabbit cytochrome B5. factors determining the heterogeneous binding…”. Solution nmr, 1 ligand (HEM), 1 pocket (best druggability 0.60). MolNFT v1 #4444 on GenesisL1: 3D structure, binding…
- PDB
- 1DO9
- Type
- protein
- Length
- 94 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome B5
- UniProt
- P00169
- Ligands
- HEM
- Pockets
- 1 · best druggability 0.60
Structure
solution nmr · 1 distinct chain · 34% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome B5 | protein | 94 | 34% helix, 15% strand | P00169 |
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.
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 | 112 | 0.60 | 0.85 | 20 | HEM |
Compared structures
- 1DO9 · Solution structure of oxidized microsomal rabbit cytochrome B5. factors determining the… · the same entry in another collection · chain A against A, TM-score 1.00
- P00169 · AlphaFold monomer V2.0 prediction for cytochrome B5 (P00169) · a predicted model of the same protein · chain A against A, TM-score 0.81
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 P00169
- Elsewhere: RCSB PDB 1DO9 · PDBe 1DO9 · UniProt P00169
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.