Structure of PDB 1zjp Chain A

Receptor sequence
>1zjpA (length=261) Species: 9606 (Homo sapiens) [Search protein sequence]
VSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQN
TTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVT
LGTGRQLSVLEVERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGTLHP
SFYGSSREAFTYERRPQSQAYIPKDEGDFYYMGAFFGGSVQEVQRLTRAC
HQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVLSPEYLWDQQLLGWPA
VLRKLRFTAVP
3D structure
PDB1zjp Differential Recognition of the Type I and II H Antigen Acceptors by the Human ABO(H) Blood Group A and B Glycosyltransferases.
ChainA
Resolution1.59 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H233 M266 W300 E303 A343
Catalytic site (residue number reindexed from 1) H149 M182 W216 E219 A259
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 MN A D211 D213 D127 D129
BS02 DR4 A M214 H233 P234 S235 F236 T245 M266 W300 E303 W325 A343 M130 H149 P150 S151 F152 T161 M182 W216 E219 W241 A259
BS03 UDP A F121 I123 Y126 D211 V212 D213 F58 I60 Y63 D127 V128 D129
Gene Ontology
Molecular Function
GO:0016758 hexosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1zjp, PDBe:1zjp, PDBj:1zjp
PDBsum1zjp
PubMed16326711
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

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