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3RHZ

Structure and functional analysis of a new subfamily of glycosyltransferases required for glycosylation of serine-rich streptococcal adhesions

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0006486biological_processprotein glycosylation
A0008194molecular_functionUDP-glycosyltransferase activity
A0016757molecular_functionglycosyltransferase activity
A0035251molecular_functionUDP-glucosyltransferase activity
B0000166molecular_functionnucleotide binding
B0006486biological_processprotein glycosylation
B0008194molecular_functionUDP-glycosyltransferase activity
B0016757molecular_functionglycosyltransferase activity
B0035251molecular_functionUDP-glucosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE UDP A 7517
ChainResidue
ATHR16
ALYS246
ASER249
AHOH460
AHOH462
AHOH530
APRO174
AARG179
ATYR195
ATYR211
AARG212
AASP214
ASER244
ATYR245

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE UDP B 7517
ChainResidue
BTHR16
BPRO174
BARG179
BTYR195
BTYR211
BARG212
BASP214
BSER244
BTYR245
BLYS246
BSER249

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00841, ECO:0000269|PubMed:21653318, ECO:0007744|PDB:3QKW, ECO:0007744|PDB:3RHZ
ChainResidueDetails
ASER244
BTHR16
BARG179
BSER244
ATHR16
AARG179

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21653318, ECO:0007744|PDB:3QKW, ECO:0007744|PDB:3RHZ
ChainResidueDetails
ATYR211
BTYR211

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PDB entries from 2024-06-12

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