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3I99

The crystal structure of the UDP-N-acetylenolpyruvoylglucosamine reductase from the Vibrio cholerae O1 biovar Tor

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 Residues34
DetailsBINDING SITE FOR RESIDUE FAD A 358
ChainResidue
ATHR24
AASN79
AILE124
APRO125
AGLY126
ACYS127
ASER130
AILE133
AILE136
AGLY137
AARG173
AILE59
AALA185
AVAL186
AVAL187
AARG227
AASN239
AALA240
AGLY241
AARG339
AHOH366
AHOH375
AILE60
AHOH396
AHOH405
AHOH407
AHOH455
AHOH457
AGLY61
ALYS62
AGLY63
ASER64
AASN65
AMSE66

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 359
ChainResidue
ATYR172
AARG173
ASER242
APHE244
ALYS245
AASN246
ALEU302
AGLU337
AHOH401

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 360
ChainResidue
ATHR10
AGLU38
ASER39
AASP42

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00037
ChainResidueDetails
AARG173
AGLU337

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00037
ChainResidueDetails
ASER242

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PDB entries from 2024-06-12

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