Structure of PDB 1lzi Chain A

Receptor sequence
>1lziA (length=264) Species: 9606 (Homo sapiens) [Search protein sequence]
MVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQ
NTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRV
TLGTGRQLSVLEVRCERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGT
LHPGFYGSSREAFTYERRPQSQAYIPKDEGDFYYLGGFFGGSVQEVQRLT
RACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVLSPEYLWDQQLLG
WPAVLRKLRFTAVP
3D structure
PDB1lzi The structural basis for specificity in human ABO(H) blood group biosynthesis.
ChainA
Resolution1.35 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 L266 W300 E303 A343
Catalytic site (residue number reindexed from 1) H152 L185 W219 E222 A262
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 D130 D132
BS02 UDP A F121 A122 I123 Y126 D211 V212 D213 F59 A60 I61 Y64 D130 V131 D132
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:1lzi, PDBe:1lzi, PDBj:1lzi
PDBsum1lzi
PubMed12198488
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

[Back to BioLiP]