Structure of PDB 4c2s Chain B

Receptor sequence
>4c2sB (length=290) Species: 9606 (Homo sapiens) [Search protein sequence]
VSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQN
TTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQLAAVPRVT
LGTGRQLSVLEVRAYKRWQDVSMRRMEMISDFCERRFLSEVDYLVCVDVD
MEFRDHVGVEILTPLFGTLHPGFYGSSREAFTYERRPQSQAYIPKDEGDF
YYLGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRH
KPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRN
3D structure
PDB4c2s Structural and Biochemical Characterization of the Human Blood Group a and B Galactosyltransferases Posessing the Pro156Leu Mutation
ChainB
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) H170 L203 W237 E240 A280 R289
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 B H233 F236 T245 Y264 W300 E303 H170 F173 T182 Y201 W237 E240
BS02 FUC B D326 H348 D263 H285
BS03 MN B D211 D213 D148 D150
BS04 UDP B F121 A122 I123 Y126 V184 R188 D211 V212 D213 K346 R352 F58 A59 I60 Y63 V121 R125 D148 V149 D150 K283 R289
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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