Structure of PDB 4c2s Chain A

Receptor sequence
>4c2sA (length=291) Species: 9606 (Homo sapiens) [Search protein sequence]
MVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQ
NTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQLAAVPRV
TLGTGRQLSVLEVRAYKRWQDVSMRRMEMISDFCERRFLSEVDYLVCVDV
DMEFRDHVGVEILTPLFGTLHPGFYGSSREAFTYERRPQSQAYIPKDEGD
FYYLGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLR
HKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRN
3D structure
PDB4c2s Structural and Biochemical Characterization of the Human Blood Group a and B Galactosyltransferases Posessing the Pro156Leu Mutation
ChainA
Resolution2.48 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 L266 W300 E303 A343 R352
Catalytic site (residue number reindexed from 1) H171 L204 W238 E241 A281 R290
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 DLG A H233 G235 F236 T245 W300 E303 H171 G173 F174 T183 W238 E241
BS02 FUC A D326 H348 D264 H286
BS03 MN A D211 D213 D149 D151
BS04 UDP A F121 I123 Y126 V184 R188 D211 V212 D213 K346 R352 F59 I61 Y64 V122 R126 D149 V150 D151 K284 R290
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:4c2s, PDBe:4c2s, PDBj:4c2s
PDBsum4c2s
PubMed
UniProtP16442|BGAT_HUMAN Histo-blood group ABO system transferase (Gene Name=ABO)

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