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1F0K

THE 1.9 ANGSTROM CRYSTAL STRUCTURE OF E. COLI MURG

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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 365
ChainResidue
BALA77
BPRO78
BLEU79
BARG80
BHOH388
BHOH410
BHOH428

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
ATHR16
BALA264
AASN128
AARG164
AILE245
AALA264
BTHR16
BASN128
BARG164
BILE245

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00033
ChainResidueDetails
ASER192
BSER192

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12538870, ECO:0007744|PDB:1NLM
ChainResidueDetails
AGLN288
BGLN288

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PDB entries from 2024-11-06

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