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Crystal structure of ubig

Analyse Crystal structure of ubig in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4KDC
Type: protein
Length: 217 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-demethylubiquinone-9 3-methyltransferase
EC: 2.1.1.64, 2.1.1.222
UniProt: P17993
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-demethylubiquinone-9 3-methyltransferase (EC 2.1.1.64, 2.1.1.222)	protein	217	41% helix, 25% strand	P17993

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	59	0.72	0.98	19	empty
2	115	0.64	0.88	20	empty

Compared structures

4KDC · Crystal Structure of UBIG · the same entry in another collection · chain A against A, TM-score 1.00
P17993 · AlphaFold monomer V2.0 prediction for ubiquinone biosynthesis O-methyltransferase (P17993) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 P17993
Elsewhere: RCSB PDB 4KDC · PDBe 4KDC · UniProt P17993

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