Research workbench

X-ray structure of a KIJD3 in complex with FMN and dtdp-3-amino-2,3,6- trideoxy-4-keto-3-methyl-D-glucose

Analyse X-ray structure of a KIJD3 in complex with FMN and dtdp-3-amino-2,3,6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4KCF
Type: protein
Length: 407 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FAD-dependent oxidoreductase
UniProt: B3TMR1
Ligands: AKM, FMN
Pockets: 1 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FAD-dependent oxidoreductase	protein	407	56% helix, 13% strand	B3TMR1

Ligands and binding sites

AKM · [(2R,4S,6R)-4-azanyl-4,6-dimethyl-5,5-bis(oxidanyl)oxan-2-yl] [[(2R,3S,5R)-5-[5-methyl-2,4-bis(oxidanylidene)pyrimidin-1-yl]-3-oxidanyl-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] hydrogen phosphate · ligand · chains A
FMN · Flavin mononucleotide · ligand · 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	864	0.81	0.83	88	AKM, FMN

Compared structures

4KCF · X-ray Structure of a KijD3 in Complex with FMN and… · 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 B3TMR1
Elsewhere: RCSB PDB 4KCF · PDBe 4KCF · UniProt B3TMR1

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