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Naturally occurring mutation of humna ABO(H) galactosyltransferase in complex with udp: GTB/M214T_UDP

Analyse Naturally occurring mutation of humna ABO(H) galactosyltransferase in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O1H
Type: protein
Length: 262 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Abo glycosyltransferase
UniProt: Q70V27
Ligands: UDP, HG, MN
Pockets: 2 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Abo glycosyltransferase	protein	262	30% helix, 21% strand	Q70V27

Ligands and binding sites

UDP · Uridine-5'-diphosphate · ligand · chains A
HG · Mercury (II) ion · metal · 5 copies · chains A
MN · Manganese (II) ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	230	0.50	0.75	28	HG, UDP
2	65	0.31	0.74	13	empty

Compared structures

2O1H · Naturally occurring mutation of Humna ABO(H) Galactosyltransferase in complex with UDP… · 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 Q70V27
Elsewhere: RCSB PDB 2O1H · PDBe 2O1H · UniProt Q70V27

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