Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2VHW

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000286	molecular_function	alanine dehydrogenase activity
A	0001666	biological_process	response to hypoxia
A	0005576	cellular_component	extracellular region
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006524	biological_process	alanine catabolic process
A	0009274	cellular_component	peptidoglycan-based cell wall
A	0016491	molecular_function	oxidoreductase activity
A	0042853	biological_process	L-alanine catabolic process
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0000286	molecular_function	alanine dehydrogenase activity
B	0001666	biological_process	response to hypoxia
B	0005576	cellular_component	extracellular region
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006524	biological_process	alanine catabolic process
B	0009274	cellular_component	peptidoglycan-based cell wall
B	0016491	molecular_function	oxidoreductase activity
B	0042853	biological_process	L-alanine catabolic process
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0000286	molecular_function	alanine dehydrogenase activity
C	0001666	biological_process	response to hypoxia
C	0005576	cellular_component	extracellular region
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006524	biological_process	alanine catabolic process
C	0009274	cellular_component	peptidoglycan-based cell wall
C	0016491	molecular_function	oxidoreductase activity
C	0042853	biological_process	L-alanine catabolic process
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0000286	molecular_function	alanine dehydrogenase activity
D	0001666	biological_process	response to hypoxia
D	0005576	cellular_component	extracellular region
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006524	biological_process	alanine catabolic process
D	0009274	cellular_component	peptidoglycan-based cell wall
D	0016491	molecular_function	oxidoreductase activity
D	0042853	biological_process	L-alanine catabolic process
D	0046872	molecular_function	metal ion binding
E	0000166	molecular_function	nucleotide binding
E	0000286	molecular_function	alanine dehydrogenase activity
E	0001666	biological_process	response to hypoxia
E	0005576	cellular_component	extracellular region
E	0005829	cellular_component	cytosol
E	0005886	cellular_component	plasma membrane
E	0006524	biological_process	alanine catabolic process
E	0009274	cellular_component	peptidoglycan-based cell wall
E	0016491	molecular_function	oxidoreductase activity
E	0042853	biological_process	L-alanine catabolic process
E	0046872	molecular_function	metal ion binding
F	0000166	molecular_function	nucleotide binding
F	0000286	molecular_function	alanine dehydrogenase activity
F	0001666	biological_process	response to hypoxia
F	0005576	cellular_component	extracellular region
F	0005829	cellular_component	cytosol
F	0005886	cellular_component	plasma membrane
F	0006524	biological_process	alanine catabolic process
F	0009274	cellular_component	peptidoglycan-based cell wall
F	0016491	molecular_function	oxidoreductase activity
F	0042853	biological_process	L-alanine catabolic process
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A1372

Chain	Residue
A	GLU323
A	HIS327
A	HOH2190
A	HOH2191
A	HOH2192

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B1371

Chain	Residue
B	HOH2279
D	HOH2098
B	HIS327
B	HOH2014
B	HOH2274
B	HOH2277

site_id	AC3
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAI E1374

Chain	Residue
E	LEU130
E	MET133
E	SER134
E	ALA137
E	GLY177
E	THR178
E	ALA179
E	ASP198
E	LYS203
E	SER220
E	ALA238
E	VAL239
E	LEU240
E	LEU249
E	ILE267
E	ASP270
E	GLN271
E	VAL298
E	ALA299
E	ASN300
E	MET301
E	PRO302
E	HOH2093
E	HOH2123
E	HOH2135
E	HOH2136
E	HOH2137
E	HOH2154
E	HOH2193
E	HOH2194
E	HOH2195

site_id	AC4
Number of Residues	34
Details	BINDING SITE FOR RESIDUE NAI F1374

Chain	Residue
F	LEU130
F	MET133
F	SER134
F	ALA137
F	GLY177
F	THR178
F	ALA179
F	ASP198
F	LYS203
F	SER220
F	ALA238
F	VAL239
F	LEU240
F	LEU249
F	ILE267
F	ASP270
F	GLN271
F	VAL298
F	ALA299
F	ASN300
F	MET301
F	PRO302
F	HOH2145
F	HOH2164
F	HOH2176
F	HOH2272
F	HOH2273
F	HOH2274
F	HOH2275
F	HOH2276
F	HOH2277
F	HOH2278
F	HOH2279
F	HOH2280

site_id	AC5
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAI A1373

Chain	Residue
A	HOH2216
A	HOH2217
A	HOH2218
A	HOH2219
A	MET133
A	SER134
A	ALA137
A	GLY177
A	THR178
A	ALA179
A	LEU197
A	ASP198
A	LYS203
A	SER220
A	ALA238
A	VAL239
A	LEU240
A	LEU249
A	ILE267
A	ASP270
A	VAL298
A	ALA299
A	MET301
A	PRO302
A	HOH2117
A	HOH2149
A	HOH2215

site_id	AC6
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAI B1372

Chain	Residue
B	MET133
B	SER134
B	ALA137
B	GLY177
B	THR178
B	ALA179
B	LEU197
B	ASP198
B	LYS203
B	SER220
B	ALA238
B	VAL239
B	LEU240
B	LEU249
B	ILE267
B	ASP270
B	VAL298
B	ALA299
B	ASN300
B	MET301
B	PRO302
B	HOH2183
B	HOH2206
B	HOH2219
B	HOH2220
B	HOH2306
B	HOH2307
B	HOH2308
B	HOH2309
B	HOH2310

site_id	AC7
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAI C1372

Chain	Residue
C	MET133
C	SER134
C	ALA137
C	GLY177
C	THR178
C	ALA179
C	ASP198
C	LYS203
C	SER220
C	ALA238
C	VAL239
C	LEU240
C	LEU249
C	ILE267
C	ASP270
C	VAL298
C	ALA299
C	MET301
C	PRO302
C	HOH2158
C	HOH2206
C	HOH2207
C	HOH2208
C	HOH2209
C	HOH2210
C	HOH2211

site_id	AC8
Number of Residues	29
Details	BINDING SITE FOR RESIDUE NAI D1371

Chain	Residue
D	MET133
D	SER134
D	ALA137
D	GLY177
D	THR178
D	ALA179
D	ASP198
D	ILE199
D	LYS203
D	SER220
D	ALA238
D	VAL239
D	LEU240
D	LEU249
D	ILE267
D	ASP270
D	GLN271
D	VAL298
D	ALA299
D	MET301
D	PRO302
D	HOH2210
D	HOH2239
D	HOH2291
D	HOH2292
D	HOH2293
D	HOH2294
D	HOH2295
D	HOH2297

Functional Information from PROSITE/UniProt

site_id	PS00836
Number of Residues	27
Details	ALADH_PNT_1 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 1. GIPtEtknNEf..RVAiTPaGVaeLtRrG

Chain	Residue	Details
A	GLY4-GLY30

site_id	PS00837
Number of Residues	26
Details	ALADH_PNT_2 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 2. VIGAGtAGynAariAnGMGAtVtvlD

Chain	Residue	Details
A	VAL173-ASP198

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269\|PubMed:18304579

Chain	Residue	Details
A	HIS96
E	ASP270
F	HIS96
F	ASP270
A	ASP270
B	HIS96
B	ASP270
C	HIS96
C	ASP270
D	HIS96
D	ASP270
E	HIS96

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:18304579

Chain	Residue	Details
A	ARG15
E	LYS75
F	ARG15
F	LYS75
A	LYS75
B	ARG15
B	LYS75
C	ARG15
C	LYS75
D	ARG15
D	LYS75
E	ARG15

site_id	SWS_FT_FI3
Number of Residues	54
Details	BINDING: BINDING => ECO:0000269\|PubMed:18304579, ECO:0000269\|PubMed:18491387

Chain	Residue	Details
A	SER134
B	SER134
B	THR178
B	ASP198
B	LYS203
B	SER220
B	VAL239
B	ILE267
B	ARG279
B	VAL298
C	SER134
A	THR178
C	THR178
C	ASP198
C	LYS203
C	SER220
C	VAL239
C	ILE267
C	ARG279
C	VAL298
D	SER134
D	THR178
A	ASP198
D	ASP198
D	LYS203
D	SER220
D	VAL239
D	ILE267
D	ARG279
D	VAL298
E	SER134
E	THR178
E	ASP198
A	LYS203
E	LYS203
E	SER220
E	VAL239
E	ILE267
E	ARG279
E	VAL298
F	SER134
F	THR178
F	ASP198
F	LYS203
A	SER220
F	SER220
F	VAL239
F	ILE267
F	ARG279
F	VAL298
A	VAL239
A	ILE267
A	ARG279
A	VAL298

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:18304579, ECO:0007744\|PDB:2VHX

Chain	Residue	Details
A	GLU323
E	HIS327
F	GLU323
F	HIS327
A	HIS327
B	GLU323
B	HIS327
C	GLU323
C	HIS327
D	GLU323
D	HIS327
E	GLU323

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1pjb

Chain	Residue	Details
A	GLU118
A	LYS75
A	ASP270
A	HIS96

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1pjb

Chain	Residue	Details
B	GLU118
B	LYS75
B	ASP270
B	HIS96

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1pjb

Chain	Residue	Details
C	GLU118
C	LYS75
C	ASP270
C	HIS96

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1pjb

Chain	Residue	Details
D	GLU118
D	LYS75
D	ASP270
D	HIS96

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1pjb

Chain	Residue	Details
E	GLU118
E	LYS75
E	ASP270
E	HIS96

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1pjb

Chain	Residue	Details
F	GLU118
F	LYS75
F	ASP270
F	HIS96

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)