Research workbench
Crystal structure of rat B5R in complex with FAD and NAD
Analyse Crystal structure of rat B5R in complex with FAD and NAD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IB0
- Type
- protein
- Length
- 272 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADH-cytochrome B5 reductase
- EC
- 1.6.2.2
- UniProt
- P20070
- Ligands
- FAD, NAD
- Pockets
- 5 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-cytochrome B5 reductase (EC 1.6.2.2) | protein | 272 | 24% helix, 36% strand | P20070 |
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
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 339 | 0.61 | 0.78 | 41 | FAD, NAD |
| 2 | 129 | 0.40 | 0.75 | 31 | empty |
| 3 | 83 | 0.33 | 0.74 | 14 | empty |
| 4 | 62 | 0.32 | 0.76 | 19 | empty |
| 5 | 52 | 0.30 | 0.76 | 17 | empty |
Compared structures
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 P20070
- Elsewhere: RCSB PDB 1IB0 · PDBe 1IB0 · UniProt P20070
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