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4LY8

dihydrodipicolinate synthase from C. jejuni with pyruvate bound to the active site

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
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
B0008652biological_processamino acid biosynthetic process
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
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0008652biological_processamino acid biosynthetic process
C0008840molecular_function4-hydroxy-tetrahydrodipicolinate synthase activity
C0009085biological_processlysine biosynthetic process
C0009089biological_processlysine biosynthetic process via diaminopimelate
C0016829molecular_functionlyase activity
C0019877biological_processdiaminopimelate biosynthetic process
C0044281biological_processsmall molecule metabolic process
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0008652biological_processamino acid biosynthetic process
D0008840molecular_function4-hydroxy-tetrahydrodipicolinate synthase activity
D0009085biological_processlysine biosynthetic process
D0009089biological_processlysine biosynthetic process via diaminopimelate
D0016829molecular_functionlyase activity
D0019877biological_processdiaminopimelate biosynthetic process
D0044281biological_processsmall molecule metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 301
ChainResidue
AHIS223
APHE224

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PGE A 302
ChainResidue
AGLY20
AARG272
APGE304

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 303
ChainResidue
AASN161
AALA127
AGLN128
AVAL130
AASP131

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE A 304
ChainResidue
APHE271
AARG272
ALEU273
APGE302
AHOH434

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PGE A 305
ChainResidue
AMET186
ALYS204

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 306
ChainResidue
AASP238
AGLU239
ATYR241
AASN242
BHIS181

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE A 307
ChainResidue
AALA263
AGLY264
AILE295
AGLY297
AHOH523

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 308
ChainResidue
AGLU36
DEDO303

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 309
ChainResidue
ASER200
AGLY202
ATYR230
BLYS234

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 310
ChainResidue
ATHR149
AASP150
AASP177
AHIS181
AACT312

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 311
ChainResidue
APRO278

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 312
ChainResidue
AARG157
AGOL310

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 A 313
ChainResidue
AGLN117
ATYR120
AASP150
ALYS154

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 314
ChainResidue
ASER51
ALEU54
AHIS56
AHIS59
AHOH444
AHOH488

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGE B 301
ChainResidue
BGLN117
BASP150
BTHR151
BLYS154

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 302
ChainResidue
BARG142
BKPI166
BPHE248
BASN252
BHOH472

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGE B 303
ChainResidue
BMET186
BLYS204
BLEU226
CLYS231

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 304
ChainResidue
BILE7
BLEU226

site_idCC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PGE B 305
ChainResidue
BTYR261
BLEU262

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGE B 306
ChainResidue
BHIS223
BPHE224
BASP227
DHOH496

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 307
ChainResidue
BSER51
BLEU54
BHIS56
BHIS59

site_idCC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 308
ChainResidue
BASP150
BASP177
BHIS181

site_idCC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 309
ChainResidue
BARG29
BARG33
BPHE298

site_idCC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PG4 C 301
ChainResidue
CGLN117
CTYR120
CTHR151
CLYS154
CHOH511
CHOH527

site_idCC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO C 302
ChainResidue
CVAL90
CLYS94

site_idCC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO C 303
ChainResidue
CGLY91
CLEU92

site_idCC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGE C 304
ChainResidue
CILE7
CMET186
CLYS204
CLEU226

site_idDC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO C 305
ChainResidue
CALA263
CGLY297

site_idDC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO C 306
ChainResidue
CPHE224

site_idDC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO C 307
ChainResidue
CASP150
CASP177
CHIS181

site_idDC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGE C 308
ChainResidue
CPRO140
CGLY141
CSER169
CHOH466

site_idDC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT C 309
ChainResidue
CARG142
CPHE248
CSER251
CASN252

site_idDC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE D 301
ChainResidue
DGLN117
DTYR120
DASP150
DTHR151
DLYS154

site_idDC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL D 302
ChainResidue
DLEU54
DHIS56
DHIS59
DHOH494
DHOH538

site_idDC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO D 303
ChainResidue
AACT308
DTYR261

site_idDC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO D 304
ChainResidue
CLYS234
DSER200
DGLY202
DTYR230

site_idEC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO D 307
ChainResidue
BHOH467
DHOH438

site_idEC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO D 308
ChainResidue
DHIS223

site_idEC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO D 309
ChainResidue
DASP2
DLYS3
DPHE156
DARG184

Functional Information from PROSITE/UniProt
site_idPS00665
Number of Residues18
DetailsDHDPS_1 Dihydrodipicolinate synthase signature 1. AVVpvGTTGESatltheE
ChainResidueDetails
AALA41-GLU58

site_idPS00666
Number of Residues32
DetailsDHDPS_2 Dihydrodipicolinate synthase signature 2. YNVPgrTgceIstdtiiklfrdcenIyGVKEA
ChainResidueDetails
ATYR137-ALA168

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00418","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"HAMAP-Rule","id":"MF_00418","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00418","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsSite: {"description":"Part of a proton relay during catalysis","evidences":[{"source":"HAMAP-Rule","id":"MF_00418","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

240971

PDB entries from 2025-08-27

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