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2VHV

Crystal structure of the D270A mutant of L-alanine dehydrogenase from Mycobacterium tuberculosis in complex with NADH.

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 PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAI A1372
ChainResidue
ALEU130
ASER220
AALA238
AVAL239
ALEU240
ALEU249
AILE267
AASN270
AGLN271
AVAL298
AALA299
AMET133
AASN300
AMET301
APRO302
ASER134
AALA137
AGLY177
ATHR178
AALA179
AASP198
ALYS203

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAI B1372
ChainResidue
BMET133
BSER134
BALA137
BGLY177
BTHR178
BALA179
BASP198
BILE199
BLYS203
BSER220
BALA238
BVAL239
BLEU240
BLEU249
BILE267
BASN270
BGLN271
BVAL298
BALA299
BMET301
BPRO302

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
AASN270
BHIS96
BASN270

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

220113

PDB entries from 2024-05-22

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