MolNFT v1 · #88711 · protein
Bcsired from bacillus cereus in complex with NADPH
4D3F · Imine reductase: “Bcsired from bacillus cereus in complex with NADPH”. X-ray diffraction, 1 ligand (NAP), 2 pockets (best druggability 0.69). MolNFT v1 #88711 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4D3F
- Type
- protein
- Length
- 573 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Imine reductase
- EC
- 1.5.1.3
- Ligands
- NAP
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 59% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Imine reductase (EC 1.5.1.3) | protein | 284 | 60% helix, 15% strand | — |
| B | Imine reductase (EC 1.5.1.3) | protein | 289 | 59% helix, 15% strand | — |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 694 | 0.69 | 0.76 | 51 | NAP |
| 2 | 630 | 0.66 | 0.75 | 53 | empty |
Interfaces
1 interface between chains.
- A–B · 4200 Ų buried · 41 hydrogen bonds · protein-protein
Compared structures
- 4D3F · BcSIRED from Bacillus cereus in complex with NADPH · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 4D3F · PDBe 4D3F
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