MolNFT v1 · #61719 · protein
Crystal structure of a putative F420 dependent NADP-reductase (ARTH_0613) from arthrobacter sp. FB24 at 1.70 a resolution
3DTT · NADP oxidoreductase: “Crystal structure of a putative F420 dependent NADP-reductase (ARTH_0613) from arthrobacter sp. FB24 at 1.70…”. X-ray diffraction, 2 ligands (NAP, CL), 3 pockets (best druggability 0.56). MolNFT v1 #61719 on…
- PDB
- 3DTT
- Type
- protein
- Length
- 442 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADP oxidoreductase
- UniProt
- A0JSJ2
- Ligands
- NAP, CL
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADP oxidoreductase | protein | 220 | 44% helix, 20% strand | A0JSJ2 |
| B | NADP oxidoreductase | protein | 222 | 44% helix, 21% strand | A0JSJ2 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · chains B
- ACT · Acetate ion · additive · 2 copies · chains A, B
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 | 315 | 0.56 | 0.75 | 39 | ACT, NAP |
| 2 | 221 | 0.55 | 0.77 | 30 | ACT, NAP |
| 3 | 57 | 0.30 | 0.76 | 16 | NAP |
Interfaces
1 interface between chains.
- A–B · 1408 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 3DTT · Crystal structure of a putative f420 dependent nadp-reductase (arth_0613) from… · 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
- Every structure of UniProt A0JSJ2
- Elsewhere: RCSB PDB 3DTT · PDBe 3DTT · UniProt A0JSJ2
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