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2VOE

Crystal structure of Rv2780 from M. tuberculosis H37Rv

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000286molecular_functionL-alanine dehydrogenase (NAD+) activity
A0001666biological_processresponse to hypoxia
A0005576cellular_componentextracellular region
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006524biological_processobsolete alanine catabolic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0016491molecular_functionoxidoreductase activity
A0042853biological_processL-alanine catabolic process
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000286molecular_functionL-alanine dehydrogenase (NAD+) activity
B0001666biological_processresponse to hypoxia
B0005576cellular_componentextracellular region
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006524biological_processobsolete alanine catabolic process
B0009274cellular_componentpeptidoglycan-based cell wall
B0016491molecular_functionoxidoreductase activity
B0042853biological_processL-alanine catabolic process
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0000286molecular_functionL-alanine dehydrogenase (NAD+) activity
C0001666biological_processresponse to hypoxia
C0005576cellular_componentextracellular region
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006524biological_processobsolete alanine catabolic process
C0009274cellular_componentpeptidoglycan-based cell wall
C0016491molecular_functionoxidoreductase activity
C0042853biological_processL-alanine catabolic process
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0000286molecular_functionL-alanine dehydrogenase (NAD+) activity
D0001666biological_processresponse to hypoxia
D0005576cellular_componentextracellular region
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006524biological_processobsolete alanine catabolic process
D0009274cellular_componentpeptidoglycan-based cell wall
D0016491molecular_functionoxidoreductase activity
D0042853biological_processL-alanine catabolic process
D0046872molecular_functionmetal ion binding
E0000166molecular_functionnucleotide binding
E0000286molecular_functionL-alanine dehydrogenase (NAD+) activity
E0001666biological_processresponse to hypoxia
E0005576cellular_componentextracellular region
E0005829cellular_componentcytosol
E0005886cellular_componentplasma membrane
E0006524biological_processobsolete alanine catabolic process
E0009274cellular_componentpeptidoglycan-based cell wall
E0016491molecular_functionoxidoreductase activity
E0042853biological_processL-alanine catabolic process
E0046872molecular_functionmetal ion binding
F0000166molecular_functionnucleotide binding
F0000286molecular_functionL-alanine dehydrogenase (NAD+) activity
F0001666biological_processresponse to hypoxia
F0005576cellular_componentextracellular region
F0005829cellular_componentcytosol
F0005886cellular_componentplasma membrane
F0006524biological_processobsolete alanine catabolic process
F0009274cellular_componentpeptidoglycan-based cell wall
F0016491molecular_functionoxidoreductase activity
F0042853biological_processL-alanine catabolic process
F0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00836
Number of Residues27
DetailsALADH_PNT_1 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 1. GIPtEtknNEf..RVAiTPaGVaeLtRrG
ChainResidueDetails
AGLY4-GLY30

site_idPS00837
Number of Residues26
DetailsALADH_PNT_2 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 2. VIGAGtAGynAariAnGMGAtVtvlD
ChainResidueDetails
AVAL173-ASP198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"18304579","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18304579","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues78
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18304579","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18491387","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18304579","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VHX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pjb
ChainResidueDetails
AGLU118
ALYS75
AASP270
AHIS96

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pjb
ChainResidueDetails
BGLU118
BLYS75
BASP270
BHIS96

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pjb
ChainResidueDetails
CGLU118
CLYS75
CASP270
CHIS96

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pjb
ChainResidueDetails
DGLU118
DLYS75
DASP270
DHIS96

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pjb
ChainResidueDetails
EGLU118
ELYS75
EASP270
EHIS96

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pjb
ChainResidueDetails
FGLU118
FLYS75
FASP270
FHIS96

249697

PDB entries from 2026-02-25

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