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1DRU

ESCHERICHIA COLI DHPR/NADH COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0008839molecular_function4-hydroxy-tetrahydrodipicolinate reductase
A0009085biological_processlysine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0016491molecular_functionoxidoreductase activity
A0016726molecular_functionoxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
A0019877biological_processdiaminopimelate biosynthetic process
A0042802molecular_functionidentical protein binding
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE NAD A 301
ChainResidue
AGLY12
AGLY15
AARG16
AMET17
AGLU38
AARG39
APHE79
ATHR80
AARG81
AGLY84
AGLY102
ATHR103
ATHR104
AALA126
AALA127
AASN128
APHE129
APHE243
AHOH401

site_idBIN
Number of Residues15
DetailsDINUCLEOTIDE BINDING SITE
ChainResidue
AGLY12
AGLY102
ATHR104
AALA126
AALA127
APHE129
AARG240
AGLY15
AARG16
AMET17
AGLU38
AARG39
ATHR80
AARG81
AGLY84

Functional Information from PROSITE/UniProt
site_idPS01298
Number of Residues18
DetailsDAPB Dihydrodipicolinate reductase signature. EIiEaHhrhKvDapSGTA
ChainResidueDetails
AGLU154-ALA171

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor
ChainResidueDetails
AHIS159

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
ALYS163

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:7893645, ECO:0007744|PDB:1DIH
ChainResidueDetails
AARG16
AARG39
AGLY102
APHE129
AARG240
AGLY12

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8873595, ECO:0000269|PubMed:9398235, ECO:0007744|PDB:1ARZ, ECO:0007744|PDB:1DRU
ChainResidueDetails
AGLU38
ATHR80
AALA126
AGLY15

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AGLY169
AHIS160

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:9398235, ECO:0007744|PDB:1ARZ
ChainResidueDetails
APHE243
ALYS163

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 402
ChainResidueDetails
AHIS159activator, proton shuttle (general acid/base)
ALYS163activator, electrostatic stabiliser, proton shuttle (general acid/base)

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PDB entries from 2024-05-15

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