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WELO5 G166D variant bound to FE(II), 2-oxoglutarate, and 12- epifischerindole U

Analyse WELO5 G166D variant bound to FE(II), 2-oxoglutarate, and 12- epifischerindole U in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5IQU
Type: protein
Length: 267 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: WELO5
UniProt: A0A067YX61
Ligands: AKG, 6CU, FE2
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	WELO5	protein	267	29% helix, 28% strand	A0A067YX61

Ligands and binding sites

AKG · 2-oxoglutaric acid · ligand · chains A
6CU · (6aS,9R,10R,10aS)-9-ethyl-10-isocyano-6,6,9-trimethyl-5,6,6a,7,8,9,10,10a-octahydroindeno[2,1-b]indole · ligand · chains A
FE2 · Fe (II) ion · metal · 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	438	0.70	0.81	49	FE2, AKG, 6CU

Compared structures

5IQU · WelO5 G166D variant bound to Fe(II), 2-oxoglutarate, and 12-epifischerindole U · 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 A0A067YX61
Elsewhere: RCSB PDB 5IQU · PDBe 5IQU · UniProt A0A067YX61

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