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2GQT

Crystal Structure of UDP-N-Acetylenolpyruvylglucosamine Reductase (MurB) from Thermus caldophilus

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008360biological_processregulation of cell shape
A0008762molecular_functionUDP-N-acetylmuramate dehydrogenase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0051301biological_processcell division
A0071555biological_processcell wall organization
A0071949molecular_functionFAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 501
ChainResidue
AVAL140
AGLU256
AHOH617
AHOH618
AHOH637
AHOH669

site_idAC2
Number of Residues36
DetailsBINDING SITE FOR RESIDUE FAD A 601
ChainResidue
AASN46
AGLY47
ASER48
AASN49
ALEU50
AILE104
APRO105
AALA106
AGLN107
AGLY109
AGLY110
AALA111
ALYS113
AMET114
AALA116
AGLY117
AARG151
AGLY159
AILE160
AVAL161
AARG187
ASER195
AALA196
AGLY197
AGLU264
AHOH609
AHOH625
AHOH639
AHOH661
AHOH766
AHOH789
AHOH846
AHOH1021
ATHR15
AVAL43
AGLY45

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00037
ChainResidueDetails
AARG151

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00037
ChainResidueDetails
ACYS198

237735

PDB entries from 2025-06-18

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