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4PLT

Crystal structure of ancestral apicomplexan malate dehydrogenase with oxamate.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
A0006089biological_processlactate metabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019752biological_processcarboxylic acid metabolic process
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
B0006089biological_processlactate metabolic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019752biological_processcarboxylic acid metabolic process
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
C0006089biological_processlactate metabolic process
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0019752biological_processcarboxylic acid metabolic process
D0000166molecular_functionnucleotide binding
D0003824molecular_functioncatalytic activity
D0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
D0006089biological_processlactate metabolic process
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0019752biological_processcarboxylic acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues34
Detailsbinding site for residue NAI B 401
ChainResidue
BGLY13
BTHR79
BALA80
BGLY81
BILE82
BPRO83
BASN102
BILE105
BVAL125
BASN127
BLEU129
BASN14
BMET150
BLEU154
BHIS182
BALA237
BPRO241
BOXM402
BHOH519
BHOH522
BHOH525
BHOH549
BILE15
BHOH564
BHOH612
BHOH619
BHOH632
BHOH733
BPHE34
BASP35
BILE36
BVAL37
BMET40
BTYR67

site_idAC2
Number of Residues10
Detailsbinding site for residue OXM B 402
ChainResidue
BTRP93
BARG95
BASN127
BARG158
BHIS182
BGLY225
BALA237
BNAI401
BHOH550
BHOH612

site_idAC3
Number of Residues33
Detailsbinding site for residue NAI A 401
ChainResidue
AGLY13
AASN14
AILE15
APHE34
AASP35
AILE36
AVAL37
AMET40
ATYR67
ATHR79
AALA80
AGLY81
AILE82
APRO83
AILE105
AVAL125
ATHR126
AASN127
AMET150
ALEU154
AHIS182
AALA237
AOXM402
AHOH522
AHOH527
AHOH537
AHOH554
AHOH561
AHOH599
AHOH625
AHOH642
AHOH661
AHOH725

site_idAC4
Number of Residues9
Detailsbinding site for residue OXM A 402
ChainResidue
ATRP93
AARG95
AASN127
AARG158
AHIS182
AALA237
ANAI401
AHOH537
AHOH544

site_idAC5
Number of Residues35
Detailsbinding site for residue NAI C 401
ChainResidue
CPRO83
CASN102
CILE105
CVAL125
CTHR126
CASN127
CLEU129
CMET150
CLEU154
CHIS182
CALA237
CPRO241
COXM402
CHOH527
CHOH545
CHOH563
CHOH572
CHOH573
CHOH583
CHOH589
CHOH604
CHOH673
CGLY13
CASN14
CILE15
CPHE34
CASP35
CILE36
CVAL37
CMET40
CTYR67
CTHR79
CALA80
CGLY81
CILE82

site_idAC6
Number of Residues9
Detailsbinding site for residue OXM C 402
ChainResidue
CTRP93
CARG95
CASN127
CARG158
CHIS182
CGLY225
CNAI401
CHOH544
CHOH572

site_idAC7
Number of Residues34
Detailsbinding site for residue NAI D 401
ChainResidue
DGLY13
DASN14
DILE15
DPHE34
DASP35
DILE36
DVAL37
DMET40
DTHR79
DALA80
DGLY81
DILE82
DPRO83
DLEU98
DASN102
DILE105
DVAL125
DASN127
DMET150
DLEU154
DHIS182
DALA237
DPRO241
DOXM402
DHOH520
DHOH548
DHOH549
DHOH556
DHOH566
DHOH574
DHOH609
DHOH619
DHOH629
DHOH652

site_idAC8
Number of Residues8
Detailsbinding site for residue OXM D 402
ChainResidue
DTRP93
DARG95
DASN127
DARG158
DHIS182
DNAI401
DHOH524
DHOH566

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PDB entries from 2025-06-18

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