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1MBT

OXIDOREDUCTASE

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 Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 600
ChainResidue
ATYR158
AASN233
ALYS262

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE FAD A 401
ChainResidue
AASN51
AVAL52
AASN65
AILE110
APRO111
AGLY112
ACYS113
ASER116
AILE119
AGLN120
AILE122
AGLY123
AARG159
AILE173
AARG214
AASN226
AGLY228
AGLU325
AARG327
AILE45
ALEU46
AGLY47
AGLU48
AGLY49
ASER50

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AARG159
AGLU325

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
ASER229

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ATYR190

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1mbb
ChainResidueDetails
AGLU325
ASER229
AARG159

site_idMCSA1
Number of Residues3
DetailsM-CSA 353
ChainResidueDetails
AARG159attractive charge-charge interaction, electrostatic stabiliser, increase electrophilicity
ASER229activator, proton acceptor, proton donor
AGLU325activator, attractive charge-charge interaction, electrostatic stabiliser, increase basicity, increase electrophilicity, proton acceptor, proton donor

222415

PDB entries from 2024-07-10

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