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1NLM

CRYSTAL STRUCTURE OF MURG:GLCNAC COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0005975biological_processcarbohydrate metabolic process
A0008360biological_processregulation of cell shape
A0009252biological_processpeptidoglycan biosynthetic process
A0016757molecular_functionglycosyltransferase activity
A0016758molecular_functionhexosyltransferase activity
A0030259biological_processlipid glycosylation
A0050511molecular_functionundecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity
A0051301biological_processcell division
A0051991molecular_functionUDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol 4-beta-N-acetylglucosaminlytransferase activity
A0071555biological_processcell wall organization
A1901137biological_processcarbohydrate derivative biosynthetic process
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0005975biological_processcarbohydrate metabolic process
B0008360biological_processregulation of cell shape
B0009252biological_processpeptidoglycan biosynthetic process
B0016757molecular_functionglycosyltransferase activity
B0016758molecular_functionhexosyltransferase activity
B0030259biological_processlipid glycosylation
B0050511molecular_functionundecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity
B0051301biological_processcell division
B0051991molecular_functionUDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol 4-beta-N-acetylglucosaminlytransferase activity
B0071555biological_processcell wall organization
B1901137biological_processcarbohydrate derivative biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE UD1 A 401
ChainResidue
AGLY18
AGLY263
AALA264
ALEU265
ATHR266
AGLU269
APHE282
AGLN288
AGLN289
AASN292
AGOL502
AASN128
AHOH515
AHOH526
AHOH531
AARG164
AGLY191
ASER192
AGLN218
APHE244
AILE245
AMET248

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE UD1 B 402
ChainResidue
BTHR16
BGLY17
BGLY18
BPHE21
BARG164
BGLY191
BSER192
BGLN193
BGLN218
BPHE244
BILE245
BMET248
BGLY263
BALA264
BLEU265
BTHR266
BGLU269
BHOH510
BHOH516
BHOH525

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
APHE149
AGLY160
AASN161
ASER268
AALA271
AALA337
AHOH506
AHOH510

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
APHE21
AARG164
AUD1401

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
AGLY194
AALA195
AARG261
APHE282
AHOH525
AHOH534

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL B 504
ChainResidue
BSER117

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00033, ECO:0000269|PubMed:12538870, ECO:0007744|PDB:1NLM
ChainResidueDetails
AGLY17
BLEU265
AGLY129
ATHR165
AASP246
ALEU265
BGLY17
BGLY129
BTHR165
BASP246

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00033
ChainResidueDetails
AGLN193
BGLN193

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12538870, ECO:0007744|PDB:1NLM
ChainResidueDetails
AGLN289
BGLN289

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PDB entries from 2024-07-24

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