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4X7M

Crystal structure of S. aureus TarM G117R mutant in complex with UDP and UDP-GlcNAc

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0019350biological_processteichoic acid biosynthetic process
A0047269molecular_functionpoly(ribitol-phosphate) N-acetylglucosaminyltransferase activity
A0071555biological_processcell wall organization
B0005737cellular_componentcytoplasm
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0019350biological_processteichoic acid biosynthetic process
B0047269molecular_functionpoly(ribitol-phosphate) N-acetylglucosaminyltransferase activity
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue UDP A 500
ChainResidue
AILE324
ASER408
AGLU411
AHOH617
AHOH624
AHOH626
AHOH630
ASER325
AARG326
ALYS331
AGLY356
ATYR382
ATHR383
APRO386
ALEU407

site_idAC2
Number of Residues23
Detailsbinding site for residue UD1 B 501
ChainResidue
BGLY16
BGLY17
BLYS59
BHIS249
BVAL250
BLEU282
BASN304
BILE324
BSER325
BARG326
BLYS331
BGLY356
BTYR382
BTHR383
BPRO386
BTYR402
BGLU403
BGLY404
BGLN405
BGLY406
BLEU407
BSER408
BGLU411

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25624472","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25697358","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25624472","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25697358","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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