Research workbench
Crystal structure of FAD-containing ferredoxin-NADP reductase from xanthomonas axonopodis pv. citri
Analyse Crystal structure of FAD-containing ferredoxin-NADP reductase from xanthomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4B4D
- Type
- protein
- Length
- 256 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
- Q8PMH0
- Ligands
- FAD, CL
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin-NADP reductase (EC 1.18.1.2) | protein | 256 | 27% helix, 31% strand | Q8PMH0 |
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 | 378 | 0.67 | 0.80 | 43 | FAD, CL |
| 2 | 141 | 0.41 | 0.74 | 22 | empty |
Compared structures
- 4B4D · Crystal structure of FAD-containing ferredoxin-NADP reductase from Xanthomonas axonopodis… · 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 Q8PMH0
- Elsewhere: RCSB PDB 4B4D · PDBe 4B4D · UniProt Q8PMH0
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