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6E66

Crystal structure of bacterial N-acetylglucosamine transferase NleB

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0016757molecular_functionglycosyltransferase activity
A0030145molecular_functionmanganese ion binding
A0030430cellular_componenthost cell cytoplasm
A0034054biological_processsymbiont-mediated suppression of host defense-related programmed cell death
A0046872molecular_functionmetal ion binding
A0085034biological_processsymbiont-mediated suppression of host NF-kappaB cascade
A0090729molecular_functiontoxin activity
A0106362molecular_functionprotein-arginine N-acetylglucosaminyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue EDO A 401
ChainResidue
ATHR179
AGLY180
AILE187

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:30979585
ChainResidueDetails
ACAS229

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:30979585, ECO:0007744|PDB:6ACI
ChainResidueDetails
AGLN24
ATYR48
ATYR195
ASER300
ASER305

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:30979585, ECO:0007744|PDB:6ACI
ChainResidueDetails
AASP199
AASN298

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-beta-linked (GlcNAc) arginine; by autocatalysis => ECO:0000269|PubMed:32432056
ChainResidueDetails
AARG-11
AARG29
AARG135
AARG269

222415

PDB entries from 2024-07-10

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