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2VOE

Crystal structure of Rv2780 from M. tuberculosis H37Rv

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000286molecular_functionalanine dehydrogenase activity
A0001666biological_processresponse to hypoxia
A0005576cellular_componentextracellular region
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006524biological_processalanine catabolic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0016491molecular_functionoxidoreductase activity
A0042853biological_processL-alanine catabolic process
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000286molecular_functionalanine dehydrogenase activity
B0001666biological_processresponse to hypoxia
B0005576cellular_componentextracellular region
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006524biological_processalanine catabolic process
B0009274cellular_componentpeptidoglycan-based cell wall
B0016491molecular_functionoxidoreductase activity
B0042853biological_processL-alanine catabolic process
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0000286molecular_functionalanine dehydrogenase activity
C0001666biological_processresponse to hypoxia
C0005576cellular_componentextracellular region
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006524biological_processalanine catabolic process
C0009274cellular_componentpeptidoglycan-based cell wall
C0016491molecular_functionoxidoreductase activity
C0042853biological_processL-alanine catabolic process
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0000286molecular_functionalanine dehydrogenase activity
D0001666biological_processresponse to hypoxia
D0005576cellular_componentextracellular region
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006524biological_processalanine catabolic process
D0009274cellular_componentpeptidoglycan-based cell wall
D0016491molecular_functionoxidoreductase activity
D0042853biological_processL-alanine catabolic process
D0046872molecular_functionmetal ion binding
E0000166molecular_functionnucleotide binding
E0000286molecular_functionalanine dehydrogenase activity
E0001666biological_processresponse to hypoxia
E0005576cellular_componentextracellular region
E0005829cellular_componentcytosol
E0005886cellular_componentplasma membrane
E0006524biological_processalanine catabolic process
E0009274cellular_componentpeptidoglycan-based cell wall
E0016491molecular_functionoxidoreductase activity
E0042853biological_processL-alanine catabolic process
E0046872molecular_functionmetal ion binding
F0000166molecular_functionnucleotide binding
F0000286molecular_functionalanine dehydrogenase activity
F0001666biological_processresponse to hypoxia
F0005576cellular_componentextracellular region
F0005829cellular_componentcytosol
F0005886cellular_componentplasma membrane
F0006524biological_processalanine 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
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:18304579
ChainResidueDetails
AHIS96
AASP270
BHIS96
BASP270
CHIS96
CASP270
DHIS96
DASP270
EHIS96
EASP270
FHIS96
FASP270

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:18304579
ChainResidueDetails
AARG15
ALYS75
BARG15
BLYS75
CARG15
CLYS75
DARG15
DLYS75
EARG15
ELYS75
FARG15
FLYS75

site_idSWS_FT_FI3
Number of Residues54
DetailsBINDING: BINDING => ECO:0000269|PubMed:18304579, ECO:0000269|PubMed:18491387
ChainResidueDetails
AILE267
AARG279
AVAL298
BSER134
BTHR178
BASP198
BLYS203
BSER220
BVAL239
BILE267
BARG279
BVAL298
CSER134
CTHR178
CASP198
CLYS203
CSER220
CVAL239
CILE267
CARG279
CVAL298
DSER134
DTHR178
DASP198
DLYS203
DSER220
DVAL239
DILE267
DARG279
DVAL298
ESER134
ETHR178
EASP198
ELYS203
ESER220
EVAL239
EILE267
EARG279
EVAL298
FSER134
FTHR178
FASP198
FLYS203
FSER220
FVAL239
FILE267
FARG279
FVAL298
ASER134
ATHR178
AASP198
ALYS203
ASER220
AVAL239

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:18304579, ECO:0007744|PDB:2VHX
ChainResidueDetails
DGLU323
DHIS327
EGLU323
EHIS327
FGLU323
FHIS327
AGLU323
AHIS327
BGLU323
BHIS327
CGLU323
CHIS327

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PDB entries from 2024-06-12

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