Research workbench

Crystal Structure of Ferredoxin reductase, BphA4 E175Q/Q177K (reduced form)

Analyse Crystal Structure of Ferredoxin reductase, BphA4 E175Q/Q177K (reduced form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4H4Q
Type: protein
Length: 399 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.95
Source: Acidovorax
Molecule: Biphenyl dioxygenase ferredoxin reductase subunit
EC: 1.18.1.3
UniProt: E7FJB9
Ligands: FAD
Pockets: 1 · best druggability 0.82

Structure

x-ray diffraction · resolution 1.95 · 1 distinct chain · 27% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Biphenyl dioxygenase ferredoxin reductase subunit (EC 1.18.1.3)	protein	399	27% helix, 30% strand	E7FJB9

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
FMT · Formic acid · additive · 5 copies · chains A

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	850	0.82	0.85	99	FAD

Compared structures

4H4Q · Crystal structure of ferredoxin reductase, BPHA4 E175Q/Q177K (reduced form) · 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 E7FJB9
Elsewhere: RCSB PDB 4H4Q · PDBe 4H4Q · UniProt E7FJB9

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.