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3DI1

Crystal structure of the Staphylococcus aureus Dihydrodipicolinate synthase-pyruvate complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008700molecular_function4-hydroxy-2-oxoglutarate aldolase activity
A0008840molecular_function4-hydroxy-tetrahydrodipicolinate synthase activity
A0009085biological_processlysine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0009436biological_processglyoxylate catabolic process
A0016829molecular_functionlyase activity
A0019877biological_processdiaminopimelate biosynthetic process
A0044281biological_processsmall molecule metabolic process
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008700molecular_function4-hydroxy-2-oxoglutarate aldolase activity
B0008840molecular_function4-hydroxy-tetrahydrodipicolinate synthase activity
B0009085biological_processlysine biosynthetic process
B0009089biological_processlysine biosynthetic process via diaminopimelate
B0009436biological_processglyoxylate catabolic process
B0016829molecular_functionlyase activity
B0019877biological_processdiaminopimelate biosynthetic process
B0044281biological_processsmall molecule metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PYR A 1001
ChainResidue
AALA11
AGLY45
ATHR46
ATHR47
AMET103
ATYR135
ALYS163

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PYR B 1002
ChainResidue
BTHR46
BTHR47
BTYR135
BLYS163
BALA11
BGLY45

Functional Information from PROSITE/UniProt
site_idPS00666
Number of Residues31
DetailsDHDPS_2 Dihydrodipicolinate synthase signature 2. YNVPsrTnmtIepetveilsqhpy.IvALKDA
ChainResidueDetails
ATYR135-ALA165

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:18671976
ChainResidueDetails
ATYR135
BTYR135

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00418, ECO:0000269|PubMed:18671976
ChainResidueDetails
ALYS163
BLYS163

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00418, ECO:0000269|PubMed:18671976
ChainResidueDetails
ATHR47
BTHR47

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00418
ChainResidueDetails
AILE206
BILE206

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Part of a proton relay during catalysis => ECO:0000305
ChainResidueDetails
ATHR46
ATYR109
BTHR46
BTYR109

221051

PDB entries from 2024-06-12

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