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2OJP

The crystal structure of a dimeric mutant of Dihydrodipicolinate synthase from E.coli- DHDPS-L197Y

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
A0042802molecular_functionidentical protein binding
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
B0042802molecular_functionidentical protein binding
B0044281biological_processsmall molecule metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1001
ChainResidue
ASER23
ALYS26
AGLY260
ALEU261
AVAL262

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1002
ChainResidue
BHOH1403
BSER23
BLYS26
BGLY260
BALA263

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

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor
ChainResidueDetails
ATYR133
BTYR133

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with substrate
ChainResidueDetails
AKGC161
BKGC161

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00418, ECO:0000269|PubMed:20353808, ECO:0000269|PubMed:22552955
ChainResidueDetails
ATHR45
AILE203
BTHR45
BILE203

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Part of a proton relay during catalysis
ChainResidueDetails
ATHR44
ATYR107
BTHR44
BTYR107

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: L-lysine inhibitor binding; via carbonyl oxygen
ChainResidueDetails
AALA49
BALA49

site_idSWS_FT_FI6
Number of Residues6
DetailsSITE: L-lysine inhibitor binding
ChainResidueDetails
AASN80
AGLU84
ATYR106
BASN80
BGLU84
BTYR106

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dhp
ChainResidueDetails
AARG138
ATYR133

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dhp
ChainResidueDetails
BARG138
BTYR133

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dhp
ChainResidueDetails
ATHR44
ATHR45

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dhp
ChainResidueDetails
BTHR44
BTHR45

site_idMCSA1
Number of Residues6
DetailsM-CSA 267
ChainResidueDetails
ATHR44hydrogen bond acceptor, hydrogen bond donor
ATYR107hydrogen bond donor
ATYR133activator, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
AARG138electrostatic stabiliser
AKGC161covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
AILE203activator, increase electrophilicity, polar interaction, steric role

site_idMCSA2
Number of Residues6
DetailsM-CSA 267
ChainResidueDetails
BTHR44hydrogen bond acceptor, hydrogen bond donor
BTYR107hydrogen bond donor
BTYR133activator, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
BARG138electrostatic stabiliser
BKGC161covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
BILE203activator, increase electrophilicity, polar interaction, steric role

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PDB entries from 2024-08-21

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