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3G0S

Dihydrodipicolinate synthase from Salmonella typhimurium LT2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0008652biological_processamino acid biosynthetic process
A0008840molecular_function4-hydroxy-tetrahydrodipicolinate synthase activity
A0009085biological_processlysine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0016597molecular_functionamino acid binding
A0016743molecular_functioncarboxyl- or carbamoyltransferase activity
A0016829molecular_functionlyase activity
A0019752biological_processcarboxylic acid metabolic process
A0019877biological_processdiaminopimelate biosynthetic process
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006520biological_processamino acid metabolic process
B0008652biological_processamino acid biosynthetic process
B0008840molecular_function4-hydroxy-tetrahydrodipicolinate synthase activity
B0009085biological_processlysine biosynthetic process
B0009089biological_processlysine biosynthetic process via diaminopimelate
B0016597molecular_functionamino acid binding
B0016743molecular_functioncarboxyl- or carbamoyltransferase activity
B0016829molecular_functionlyase activity
B0019752biological_processcarboxylic acid metabolic process
B0019877biological_processdiaminopimelate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AHOH306
AHOH430
AHOH473
AHOH474
AHOH475

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 403
ChainResidue
AVAL135
APRO136
ASER137
AHOH461

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 405
ChainResidue
ALEU101
ALYS161

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
ASER48
AALA49
AGLY78
ATYR106
AHOH390
AHOH525
AHOH543
AHOH548
BASN80
BTYR107

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
BHOH332
BHOH376
BHOH428
BHOH458
BHOH544

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 404
ChainResidue
BVAL135
BPRO136
BSER137
BALA163

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 406
ChainResidue
BLEU101
BLYS161
BHOH388

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL B 502
ChainResidue
AASN80
ATYR107
AHOH585
BSER48
BALA49
BGLY78
BVAL103
BTYR106
BHOH398
BHOH478
BHOH512

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

site_idPS00666
Number of Residues31
DetailsDHDPS_2 Dihydrodipicolinate synthase signature 2. YNVPsrTgcdMlpetvgrlaeikn.IiAIKEA
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

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1dhp
ChainResidueDetails
AARG138
ATYR133
ALYS161

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1dhp
ChainResidueDetails
BARG138
BTYR133
BLYS161

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1dhp
ChainResidueDetails
ATHR44
ALYS161
ATHR45

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1dhp
ChainResidueDetails
BTHR44
BLYS161
BTHR45

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PDB entries from 2025-06-18

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