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2GQU

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 Residues37
DetailsBINDING SITE FOR RESIDUE FAD A 501
ChainResidue
ATHR15
AILE104
APRO105
AALA106
AGLN107
AGLY109
AGLY110
AALA111
ALYS113
AMET114
AALA116
AVAL43
AGLY117
AARG151
AGLY159
AILE160
AVAL161
AARG187
ASER195
AALA196
AGLY197
AGLU264
AGLY45
AEPU601
AHOH606
AHOH619
AHOH638
AHOH662
AHOH869
AHOH971
AHOH978
AASN46
AGLY47
ASER48
AASN49
ALEU50
AGLY103

site_idAC2
Number of Residues32
DetailsBINDING SITE FOR RESIDUE EPU A 601
ChainResidue
AARG7
ATHR118
AARG119
ATYR150
AARG151
AARG187
AGLN190
AGLY197
ACYS198
AASN202
ASER207
AGLY209
AARG210
AASP213
ALYS218
AHIS231
AGLY232
AGLU262
AFAD501
AHOH665
AHOH669
AHOH680
AHOH687
AHOH754
AHOH847
AHOH868
AHOH893
AHOH915
AHOH920
AHOH978
AHOH986
AHOH997

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

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PDB entries from 2024-09-04

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