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2VHY

Crystal structure of apo L-alanine dehydrogenase from Mycobacterium tuberculosis

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
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 Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:18304579
ChainResidueDetails
AHIS96
AASP270
BHIS96
BASP270

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18304579
ChainResidueDetails
AARG15
ALYS75
BARG15
BLYS75

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:18304579, ECO:0000269|PubMed:18491387
ChainResidueDetails
ASER134
BSER134
BTHR178
BASP198
BLYS203
BSER220
BVAL239
BILE267
BARG279
BVAL298
ATHR178
AASP198
ALYS203
ASER220
AVAL239
AILE267
AARG279
AVAL298

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18304579, ECO:0007744|PDB:2VHX
ChainResidueDetails
AGLU323
AHIS327
BGLU323
BHIS327

221371

PDB entries from 2024-06-19

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