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2VHZ

Crystal structure of holo L-alanine dehydrogenase from Mycobacterium tuberculosis in the closed conformation

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 Residues32
DetailsBINDING SITE FOR RESIDUE NAI A1372
ChainResidue
AMET133
AVAL239
ALEU240
ALEU249
AILE267
AASP270
AGLN271
AVAL298
AALA299
AASN300
AMET301
ASER134
APRO302
AHOH2166
AHOH2232
AHOH2233
AHOH2234
AHOH2235
AHOH2236
AHOH2237
AHOH2238
AHOH2239
AALA137
AHOH2240
AHOH2241
AHOH2242
AGLY177
ATHR178
AALA179
AASP198
ALYS203
AALA238

site_idAC2
Number of Residues33
DetailsBINDING SITE FOR RESIDUE NAI B1372
ChainResidue
BMET133
BSER134
BALA137
BGLY177
BTHR178
BALA179
BASP198
BILE199
BLYS203
BALA238
BVAL239
BLEU240
BLEU249
BILE267
BASP270
BGLN271
BVAL298
BALA299
BASN300
BMET301
BPRO302
BHOH2178
BHOH2190
BHOH2246
BHOH2247
BHOH2248
BHOH2249
BHOH2250
BHOH2251
BHOH2252
BHOH2253
BHOH2254
BHOH2255

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
AASP198
ALYS203
ASER220
AVAL239
AILE267
AARG279
AVAL298
BSER134
BTHR178
BASP198
BLYS203
BSER220
BVAL239
BILE267
BARG279
BVAL298
ASER134
ATHR178

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

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PDB entries from 2024-06-12

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