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4MLR

dihydrodipicolinate synthase from C. jejuni, Y110F mutation with pyruvate and Lysine

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
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
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
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
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0008840molecular_function4-hydroxy-tetrahydrodipicolinate synthase activity
E0009085biological_processlysine biosynthetic process
E0009089biological_processlysine biosynthetic process via diaminopimelate
E0016829molecular_functionlyase activity
E0019877biological_processdiaminopimelate biosynthetic process
E0044281biological_processsmall molecule metabolic process
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0008840molecular_function4-hydroxy-tetrahydrodipicolinate synthase activity
F0009085biological_processlysine biosynthetic process
F0009089biological_processlysine biosynthetic process via diaminopimelate
F0016829molecular_functionlyase activity
F0019877biological_processdiaminopimelate biosynthetic process
F0044281biological_processsmall molecule metabolic process
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0008840molecular_function4-hydroxy-tetrahydrodipicolinate synthase activity
G0009085biological_processlysine biosynthetic process
G0009089biological_processlysine biosynthetic process via diaminopimelate
G0016829molecular_functionlyase activity
G0019877biological_processdiaminopimelate biosynthetic process
G0044281biological_processsmall molecule metabolic process
H0005737cellular_componentcytoplasm
H0005829cellular_componentcytosol
H0008840molecular_function4-hydroxy-tetrahydrodipicolinate synthase activity
H0009085biological_processlysine biosynthetic process
H0009089biological_processlysine biosynthetic process via diaminopimelate
H0016829molecular_functionlyase activity
H0019877biological_processdiaminopimelate biosynthetic process
H0044281biological_processsmall molecule metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE LYS A 301
ChainResidue
ASER51
AALA52
ALEU54
AHIS59
APHE110
ALYS302
DASN84
DGLU88

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE LYS A 302
ChainResidue
AGLU88
ALYS301
DSER51
DALA52
DLEU54
DHIS59
DPHE110
AASN84

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 303
ChainResidue
ATYR261

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 304
ChainResidue
ATHR149
AASP177

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 305
ChainResidue
ALYS204

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 306
ChainResidue
AHIS223
APHE224
AASP227

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE LYS B 301
ChainResidue
BSER51
BALA52
BLEU54
BHIS59
CASN84
CGLU88
CLYS301

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 B 302
ChainResidue
BGLN117
BASP150
BTHR151
BLYS154

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGE B 303
ChainResidue
BPRO183
BMET186
BGLY202
BLYS204

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE LYS C 301
ChainResidue
BASN84
BGLU88
BLYS301
CSER51
CALA52
CLEU54
CHIS59

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG4 C 302
ChainResidue
CGLN117
CTYR120
CASP150
CTHR151
CLYS154

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PGE C 303
ChainResidue
CPRO183
CMET186
CLYS204

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL C 304
ChainResidue
CPRO140

site_idBC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO D 301
ChainResidue
DARG272

site_idBC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE LYS E 301
ChainResidue
ESER51
EALA52
ELEU54
EHIS56
EHIS59
EPHE110
EHOH422
FASN84
FGLU88
FLYS301

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PGE E 302
ChainResidue
EPRO140
EGLY144

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO E 303
ChainResidue
EALA263
EILE295
EGLY297

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO E 304
ChainResidue
ETYR120
ELYS154

site_idCC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE LYS F 301
ChainResidue
EASN84
EGLU88
ELYS301
FSER51
FALA52
FLEU54
FHIS56
FHIS59
FPHE110

site_idCC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PGE F 302
ChainResidue
FGLN117
FLYS154

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT F 303
ChainResidue
EHIS56
EGLU88
FHIS56

site_idCC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE LYS G 301
ChainResidue
GSER51
GALA52
GLEU54
GHIS56
GHIS59
HASN84
HGLU88
HLYS301

site_idCC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO G 303
ChainResidue
GGLU287

site_idCC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE LYS H 301
ChainResidue
HALA52
HLEU54
HHIS59
HPHE110
GASN84
GGLU88
GLYS301
HSER51

site_idCC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PGE H 302
ChainResidue
HGLN117
HTYR120
HLYS154

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 Residues8
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00418
ChainResidueDetails
ATYR137
BTYR137
CTYR137
DTYR137
ETYR137
FTYR137
GTYR137
HTYR137

site_idSWS_FT_FI2
Number of Residues8
DetailsACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00418
ChainResidueDetails
AKPI166
BKPI166
CKPI166
DKPI166
EKPI166
FKPI166
GKPI166
HKPI166

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00418
ChainResidueDetails
ATHR48
EILE207
FTHR48
FILE207
GTHR48
GILE207
HTHR48
HILE207
AILE207
BTHR48
BILE207
CTHR48
CILE207
DTHR48
DILE207
ETHR48

site_idSWS_FT_FI4
Number of Residues16
DetailsSITE: Part of a proton relay during catalysis => ECO:0000255|HAMAP-Rule:MF_00418
ChainResidueDetails
ATHR47
ETYR111
FTHR47
FTYR111
GTHR47
GTYR111
HTHR47
HTYR111
ATYR111
BTHR47
BTYR111
CTHR47
CTYR111
DTHR47
DTYR111
ETHR47

226262

PDB entries from 2024-10-16

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