MolNFT v2 · #17044 · protein
FERREDOXIN:NADP+ reductase mutant with thr 155 replaced by gly and ala 160 replaced by thr (T155G-A160T)
1OGI · Ferredoxin--NADP+ reductase: “FERREDOXIN:NADP+ reductase mutant with thr 155 replaced by gly and ala 160 replaced by thr (T155G-A160T)”. X-ray diffraction at 1.64, 2 ligands (FAD, SO4), 2 pockets (best druggability 0.56). MolNFT v2…
- PDB
- 1OGI
- Type
- protein
- Length
- 295 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.64
- Source
- ANABAENA SP. (STRAIN PCC 7119)
- Molecule
- Ferredoxin--NADP+ reductase
- EC
- 1.18.1.2
- UniProt
- P21890
- Ligands
- FAD, SO4
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · resolution 1.64 · 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
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 247 | 0.56 | 0.77 | 29 | SO4 |
| 2 | 128 | 0.45 | 0.77 | 19 | FAD |
Compared structures
- 1OGI · FERREDOXIN:NADP+ reductase mutant with thr 155 replaced by gly and ala 160 replaced by… · 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 1OGI · PDBe 1OGI · UniProt P21890
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