Structure of PDB 3zgg Chain A

Receptor sequence
>3zggA (length=274) Species: 9606 (Homo sapiens) [Search protein sequence]
FMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRL
QNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPR
VTLGTGRQLSVLEVDVSMRRMEMISDFCFLSEVDYLVCVDVDMEFRDHVG
VEILTPLFGTLHPGFYGSSREAFTYERRPQSQAYIPKDEGDFYYGGAFFG
GSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVLSP
EYLWDQQLLGWPAVLRKLRFTAVP
3D structure
PDB3zgg Structures of a Human Blood Group Glycosyltransferase in Complex with a Photo-Activatable Udp-Gal Derivative Reveal Two Different Binding Conformations
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H233 G266 W300 E303 A343
Catalytic site (residue number reindexed from 1) H162 G195 W229 E232 A272
Enzyme Commision number 2.4.1.37: fucosylgalactoside 3-alpha-galactosyltransferase.
2.4.1.40: glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 IUG A F121 I123 Y126 V184 S185 R188 D211 V212 D213 W300 H301 D302 E303 F60 I62 Y65 V116 S117 R120 D140 V141 D142 W229 H230 D231 E232
BS02 MN A D211 D213 D140 D142
Gene Ontology
Molecular Function
GO:0016758 hexosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0016020 membrane

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:3zgg, PDBe:3zgg, PDBj:3zgg
PDBsum3zgg
PubMed25084373
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

[Back to BioLiP]