Structure of PDB 5m79 Chain A

Receptor sequence
>5m79A (length=293) Species: 9606 (Homo sapiens) [Search protein sequence]
FMVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRL
QNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPR
VTLGTGRQLSVLEVRAYKRWQDVSMRRMEMISDFCERRFLSEVDYLVCVD
VDMEFRDHVGVEILTPLFGTLHPGFYGSSREAFTYERRPQSQAYIPKDEG
DFYYGGAFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLL
RHKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRNP
3D structure
PDB5m79 Blood group synthase AAGlyB in complex with UMP and cryoprotected with glycerol
ChainA
Resolution1.3 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 G266 W300 E303 A343 R352
Catalytic site (residue number reindexed from 1) H172 G205 W239 E242 A282 R291
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 D150 D152
BS02 U5P A F121 A122 I123 Y126 V184 R188 D211 V212 D213 K346 R352 F60 A61 I62 Y65 V123 R127 D150 V151 D152 K285 R291
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:5m79, PDBe:5m79, PDBj:5m79
PDBsum5m79
PubMed
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

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