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1J4A

INSIGHTS INTO DOMAIN CLOSURE, SUBSTRATE SPECIFICITY AND CATALYSIS OF D-LACTATE DEHYDROGENASE FROM LACTOBACILLUS BULGARICUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0006089biological_processlactate metabolic process
A0008720molecular_functionD-lactate dehydrogenase (NAD+) activity
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0051287molecular_functionNAD binding
B0006089biological_processlactate metabolic process
B0008720molecular_functionD-lactate dehydrogenase (NAD+) activity
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0051287molecular_functionNAD binding
C0006089biological_processlactate metabolic process
C0008720molecular_functionD-lactate dehydrogenase (NAD+) activity
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0051287molecular_functionNAD binding
D0006089biological_processlactate metabolic process
D0008720molecular_functionD-lactate dehydrogenase (NAD+) activity
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1400
ChainResidue
AGLY155
AHIS156
AILE157
AHOH1423
AHOH1444
AHOH1479
AHOH1642

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1401
ChainResidue
AVAL79
AGLY80
AHOH1611
AGLN55
AASN78

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1402
ChainResidue
AARG236
AGLY237
AVAL261
ALYS297
AHOH1470
AHOH1554
AHOH1638

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1403
ChainResidue
ALYS18
AGLU21
ATYR31

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 2400
ChainResidue
BGLY155
BHIS156
BILE157
BHOH2416
BHOH2488
BHOH2585
BHOH2656

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 2401
ChainResidue
BASN78
BVAL79
BGLY80
BSO42403

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 2402
ChainResidue
BHIS304
BASN308
BHOH2511

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 2403
ChainResidue
BTYR53
BPHE300
BSO42401
BHOH2495
BHOH2572

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 C 3400
ChainResidue
CGLY155
CHIS156
CILE157
CHOH3415
CHOH3467
CHOH3530
CHOH3554

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 4400
ChainResidue
DGLY155
DHIS156
DILE157
DHOH4418
DHOH4449

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D 4401
ChainResidue
DGLN55
DASN78
DVAL79
DGLY80
DHOH4535
DHOH4626

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VGVVGtGHIGqvfmqimegfgak.VItYD
ChainResidueDetails
AVAL149-ASP176

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LYkqADVIsLHvPdvpaNvhMiN
ChainResidueDetails
ALEU196-ASN218

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKqDvVIVNvSRGpLVD
ChainResidueDetails
AMET225-ASP241

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsActive site: {"evidences":[{"source":"PubMed","id":"9063466","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"9063466","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12054772","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1J49","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12054772","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12054772","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1j49
ChainResidueDetails
AARG236
AASP209
AGLU265
ALYS297
AASP260

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1j49
ChainResidueDetails
BARG236
BASP209
BGLU265
BLYS297
BASP260

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1j49
ChainResidueDetails
CARG236
CASP209
CGLU265
CLYS297
CASP260

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1j49
ChainResidueDetails
DARG236
DASP209
DGLU265
DLYS297
DASP260

site_idMCSA1
Number of Residues4
DetailsM-CSA 576
ChainResidueDetails
AARG236electrostatic stabiliser
AASP260steric role
AGLU265electrostatic stabiliser
ALYS297proton acceptor, proton donor

site_idMCSA2
Number of Residues4
DetailsM-CSA 576
ChainResidueDetails
BARG236electrostatic stabiliser
BASP260steric role
BGLU265electrostatic stabiliser
BLYS297proton acceptor, proton donor

site_idMCSA3
Number of Residues4
DetailsM-CSA 576
ChainResidueDetails
CARG236electrostatic stabiliser
CASP260steric role
CGLU265electrostatic stabiliser
CLYS297proton acceptor, proton donor

site_idMCSA4
Number of Residues4
DetailsM-CSA 576
ChainResidueDetails
DARG236electrostatic stabiliser
DASP260steric role
DGLU265electrostatic stabiliser
DLYS297proton acceptor, proton donor

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PDB entries from 2025-10-22

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