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2NZW

Crystal Structure of alpha1,3-Fucosyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0006486biological_processprotein glycosylation
A0008417molecular_functionfucosyltransferase activity
A0016020cellular_componentmembrane
B0006486biological_processprotein glycosylation
B0008417molecular_functionfucosyltransferase activity
B0016020cellular_componentmembrane
C0006486biological_processprotein glycosylation
C0008417molecular_functionfucosyltransferase activity
C0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 2001
ChainResidue
BSER188
BASN189
BARG195
BASN240
BLYS250

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 C 2002
ChainResidue
CASN240
CLYS250
CHOH2267
CHOH2279
CALA187
CSER188
CASN189
CARG195

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 2003
ChainResidue
CHIS300
CLYS301
CASN302
CALA303

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:17251184, ECO:0007744|PDB:2NZY
ChainResidueDetails
AGLY94
BVAL222
BASN240
BTYR246
CGLY94
CVAL186
CARG195
CVAL222
CASN240
CTYR246
AVAL186
AARG195
AVAL222
AASN240
ATYR246
BGLY94
BVAL186
BARG195

site_idSWS_FT_FI2
Number of Residues3
DetailsSITE: Important for catalytic activity => ECO:0000269|PubMed:17251184
ChainResidueDetails
AGLU95
BGLU95
CGLU95

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PDB entries from 2024-07-10

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