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5Z1Z

The apo-structure of D-lactate dehydrogenase from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0006089biological_processlactate metabolic process
A0008720molecular_functionD-lactate dehydrogenase (NAD+) activity
A0009408biological_processresponse to heat
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019664biological_processmixed acid fermentation
A0042802molecular_functionidentical protein binding
A0051287molecular_functionNAD binding
A0051289biological_processprotein homotetramerization
A0070404molecular_functionNADH binding
B0005829cellular_componentcytosol
B0006089biological_processlactate metabolic process
B0008720molecular_functionD-lactate dehydrogenase (NAD+) activity
B0009408biological_processresponse to heat
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019664biological_processmixed acid fermentation
B0042802molecular_functionidentical protein binding
B0051287molecular_functionNAD binding
B0051289biological_processprotein homotetramerization
B0070404molecular_functionNADH binding
C0005829cellular_componentcytosol
C0006089biological_processlactate metabolic process
C0008720molecular_functionD-lactate dehydrogenase (NAD+) activity
C0009408biological_processresponse to heat
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0019664biological_processmixed acid fermentation
C0042802molecular_functionidentical protein binding
C0051287molecular_functionNAD binding
C0051289biological_processprotein homotetramerization
C0070404molecular_functionNADH binding
D0005829cellular_componentcytosol
D0006089biological_processlactate metabolic process
D0008720molecular_functionD-lactate dehydrogenase (NAD+) activity
D0009408biological_processresponse to heat
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0019664biological_processmixed acid fermentation
D0042802molecular_functionidentical protein binding
D0051287molecular_functionNAD binding
D0051289biological_processprotein homotetramerization
D0070404molecular_functionNADH binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 401
ChainResidue
AGLU21
AHOH534
AHOH543
AHOH546
CHOH401
CHOH406

site_idAC2
Number of Residues4
Detailsbinding site for residue PEG A 402
ChainResidue
APHE29
ATHR8
AGLN10
ALYS13

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. AGVIGtGKIGvamlrilkgfgmr.LLaFD
ChainResidueDetails
AALA147-ASP174

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LFseSDVIsLHcPltpeNyhLlN
ChainResidueDetails
ALEU194-ASN216

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKnGvMIVNtSRGaLID
ChainResidueDetails
AMET223-ASP239

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"P26297","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P26297","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P30901","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P26297","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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