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3PUO

Crystal structure of dihydrodipicolinate synthase from Pseudomonas aeruginosa(PsDHDPS)complexed with L-lysine at 2.65A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008840molecular_function4-hydroxy-tetrahydrodipicolinate synthase activity
A0009085biological_processlysine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0016829molecular_functionlyase activity
A0019877biological_processdiaminopimelate biosynthetic process
A0044281biological_processsmall molecule metabolic process
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008840molecular_function4-hydroxy-tetrahydrodipicolinate synthase activity
B0009085biological_processlysine biosynthetic process
B0009089biological_processlysine biosynthetic process via diaminopimelate
B0016829molecular_functionlyase activity
B0019877biological_processdiaminopimelate biosynthetic process
B0044281biological_processsmall molecule metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE LYS A 293
ChainResidue
ASER48
AALA49
ALEU51
AASP52
AVAL53
AHIS56
BASN80
BGLU84
BLYS293

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 294
ChainResidue
AARG212
AASP216
BGLU124

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE LYS A 295
ChainResidue
AMET1
AILE266
AARG267
ALEU268
ALEU270
ATHR271
ATRP272
AHOH298
BGLN117

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LYS B 293
ChainResidue
AGLU84
ALYS293
BSER48
BALA49
BLEU51
BGLU84

Functional Information from PROSITE/UniProt
site_idPS00665
Number of Residues18
DetailsDHDPS_1 Dihydrodipicolinate synthase signature 1. AIVavGTTGESatldveE
ChainResidueDetails
AALA38-GLU55

site_idPS00666
Number of Residues31
DetailsDHDPS_2 Dihydrodipicolinate synthase signature 2. YNVPgrTscdMlpetverlskvpn.IiGIKEA
ChainResidueDetails
ATYR133-ALA163

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00418
ChainResidueDetails
ATYR133
BTYR133

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00418
ChainResidueDetails
ALYS161
BLYS161

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00418
ChainResidueDetails
ATHR45
AILE203
BTHR45
BILE203

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Part of a proton relay during catalysis => ECO:0000255|HAMAP-Rule:MF_00418
ChainResidueDetails
ATHR44
ATYR107
BTHR44
BTYR107

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PDB entries from 2024-05-01

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