Research workbench
Crystal structure of ferredoxin reductase for the CYP199A2 system from rhodopseudomonas palustris
Analyse Crystal structure of ferredoxin reductase for the CYP199A2 system from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FG2
- Type
- protein
- Length
- 404 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative rubredoxin reductase
- EC
- 1.18.1.3
- UniProt
- Q6N3B2
- Ligands
- FAD
- Pockets
- 1 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | Putative rubredoxin reductase (EC 1.18.1.3) | protein | 404 | 26% helix, 31% strand | Q6N3B2 |
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 | 1118 | 0.81 | 0.83 | 106 | FAD |
Compared structures
- 3FG2 · Crystal Structure of Ferredoxin Reductase for the CYP199A2 System from Rhodopseudomonas… · the same entry in another collection · chain P against P, 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 Q6N3B2
- Elsewhere: RCSB PDB 3FG2 · PDBe 3FG2 · UniProt Q6N3B2
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