MolNFT v1 · #32323 · protein
Ferredoxin: NADP+ reductase mutant with thr 155 replaced by gly, ala 160 replaced by thr, leu 263 replaced by pro, arg 264 replaced by pro and gly 265 replaced by pro (T155G-A160T-L263P-R264P-G265P)
2BMW · Ferredoxin--NADP reductase: “Ferredoxin: NADP+ reductase mutant with thr 155 replaced by gly, ala 160 replaced by thr, leu 263 replaced by…”. X-ray diffraction, 2 ligands (FAD, SO4), 1 pocket (best druggability 0.55). MolNFT v1…
- PDB
- 2BMW
- Type
- protein
- Length
- 295 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferredoxin--NADP reductase
- EC
- 1.18.1.2
- UniProt
- P21890
- Ligands
- FAD, SO4
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 295 | 27% helix, 29% strand | P21890 |
Ligands and binding sites
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 | 326 | 0.55 | 0.75 | 40 | FAD, SO4 |
Compared structures
- 2BMW · Ferredoxin: NADP+ Reductase Mutant With Thr 155 Replaced By Gly, Ala 160 Replaced By Thr… · the same entry in another collection · chain A against A, TM-score 1.00
- P21890 · AlphaFold monomer V2.0 prediction for ferredoxin--NADP reductase (P21890) · 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 P21890
- Elsewhere: RCSB PDB 2BMW · PDBe 2BMW · UniProt P21890
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