Research workbench
2.15A resolution structure of the CS-b5R domains of human Ncb5or (NAD+ form)
Analyse 2.15A resolution structure of the CS-b5R domains of human Ncb5or (NAD+ form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MV1
- Type
- protein
- Length
- 355 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.15
- Source
- Homo sapiens
- Molecule
- Cytochrome b5 reductase 4
- EC
- 1.6.2.2
- UniProt
- Q7L1T6
- Ligands
- FAD, NAD
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · resolution 2.15 · 1 distinct chain · 18% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome b5 reductase 4 (EC 1.6.2.2) | protein | 355 | 18% helix, 39% strand | Q7L1T6 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 663 | 0.70 | 0.78 | 67 | empty |
| 2 | 342 | 0.58 | 0.76 | 41 | FAD, NAD |
| 3 | 54 | 0.32 | 0.77 | 12 | empty |
Compared structures
- 6MV1 · 2.15A resolution structure of the cs-B5R domains of human NCB5OR (NAD+ form) · the same entry in another collection · chain A against A, TM-score 1.00
- Q7L1T6 · AlphaFold monomer V2.0 prediction for cytochrome B5 reductase 4 (Q7L1T6) · 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 Q7L1T6
- Elsewhere: RCSB PDB 6MV1 · PDBe 6MV1 · UniProt Q7L1T6
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