Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1SZS

The structure of gamma-aminobutyrate aminotransferase mutant: I50Q

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
A	0005829	cellular_component	cytosol
A	0008483	molecular_function	transaminase activity
A	0009063	biological_process	amino acid catabolic process
A	0009448	biological_process	gamma-aminobutyric acid metabolic process
A	0009450	biological_process	gamma-aminobutyric acid catabolic process
A	0016740	molecular_function	transferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
A	0042450	biological_process	L-arginine biosynthetic process via ornithine
A	0042803	molecular_function	protein homodimerization activity
A	0046395	biological_process	carboxylic acid catabolic process
A	0047589	molecular_function	5-aminovalerate transaminase activity
A	0170033	biological_process	L-amino acid metabolic process
A	0170039	biological_process	proteinogenic amino acid metabolic process
B	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
B	0005829	cellular_component	cytosol
B	0008483	molecular_function	transaminase activity
B	0009063	biological_process	amino acid catabolic process
B	0009448	biological_process	gamma-aminobutyric acid metabolic process
B	0009450	biological_process	gamma-aminobutyric acid catabolic process
B	0016740	molecular_function	transferase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
B	0042450	biological_process	L-arginine biosynthetic process via ornithine
B	0042803	molecular_function	protein homodimerization activity
B	0046395	biological_process	carboxylic acid catabolic process
B	0047589	molecular_function	5-aminovalerate transaminase activity
B	0170033	biological_process	L-amino acid metabolic process
B	0170039	biological_process	proteinogenic amino acid metabolic process
C	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
C	0005829	cellular_component	cytosol
C	0008483	molecular_function	transaminase activity
C	0009063	biological_process	amino acid catabolic process
C	0009448	biological_process	gamma-aminobutyric acid metabolic process
C	0009450	biological_process	gamma-aminobutyric acid catabolic process
C	0016740	molecular_function	transferase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
C	0042450	biological_process	L-arginine biosynthetic process via ornithine
C	0042803	molecular_function	protein homodimerization activity
C	0046395	biological_process	carboxylic acid catabolic process
C	0047589	molecular_function	5-aminovalerate transaminase activity
C	0170033	biological_process	L-amino acid metabolic process
C	0170039	biological_process	proteinogenic amino acid metabolic process
D	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
D	0005829	cellular_component	cytosol
D	0008483	molecular_function	transaminase activity
D	0009063	biological_process	amino acid catabolic process
D	0009448	biological_process	gamma-aminobutyric acid metabolic process
D	0009450	biological_process	gamma-aminobutyric acid catabolic process
D	0016740	molecular_function	transferase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
D	0042450	biological_process	L-arginine biosynthetic process via ornithine
D	0042803	molecular_function	protein homodimerization activity
D	0046395	biological_process	carboxylic acid catabolic process
D	0047589	molecular_function	5-aminovalerate transaminase activity
D	0170033	biological_process	L-amino acid metabolic process
D	0170039	biological_process	proteinogenic amino acid metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 1201

Chain	Residue
A	ILE184
A	HIS188
A	ARG224

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 1202

Chain	Residue
B	LYS5
B	ARG381
B	HOH1430
B	HOH1507

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 1203

Chain	Residue
B	ARG224
B	HOH1429
B	HOH1525
B	ILE184
B	HIS188

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 1204

Chain	Residue
C	HIS188
C	ARG224
C	HOH1513

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 D 1205

Chain	Residue
D	HIS188
D	ARG224

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 1206

Chain	Residue
B	HOH1446
D	LYS5
D	ARG381
D	HOH1347

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 1207

Chain	Residue
A	LYS151
A	ASN153
A	TYR394
A	HOH1326
C	LYS192

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 1208

Chain	Residue
B	LYS151
B	ASN153
B	TYR394
D	LYS192

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 1209

Chain	Residue
B	LYS192
D	LYS151
D	ASN153
D	TYR394
D	HOH1523

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 1210

Chain	Residue
A	LYS192
A	HOH1361
C	LYS151
C	ASN153
C	TYR394

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 1211

Chain	Residue
A	GLN419
A	HOH1477
C	LYS71
C	HOH1385
D	ARG29
D	HOH1399
D	HOH1534

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 1212

Chain	Residue
A	GLN50
A	TYR138
A	ARG141
A	HOH1351
A	HOH1458
A	HOH1548
B	CYS77
B	GLN79
B	GLY296

site_id	BC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SO4 A 1213

Chain	Residue
A	CYS77
A	GLN79
A	GLY295
A	GLY296
A	HOH1448
B	GLN50
B	TYR138
B	ARG141
B	HOH1273
B	HOH1568
B	HOH1569

site_id	BC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SO4 D 1214

Chain	Residue
C	GLN50
C	ARG141
C	EDO1230
C	HOH1287
C	HOH1527
D	CYS77
D	GLN79
D	GLY295
D	GLY296
D	HOH1315
D	HOH1559

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 1215

Chain	Residue
C	GLN79
C	GLY296
D	GLN50
D	ARG141
D	HOH1305
D	HOH1432

site_id	BC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO B 1216

Chain	Residue
A	THR76
A	VAL80
A	LEU81
B	ASP45
B	ALA47
B	GLY48
B	GLY49
B	HIS57

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B 1217

Chain	Residue
B	ILE22
B	HIS23
B	ARG381
B	HOH1404

site_id	BC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EDO A 1218

Chain	Residue
A	TYR167
A	HOH1507
C	GLY164
C	HIS165
C	VAL166
C	TYR167
C	HOH1484
A	GLY164
A	HIS165
A	VAL166

site_id	CC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO B 1219

Chain	Residue
B	GLY164
B	HIS165
B	VAL166
B	TYR167
B	HOH1472
D	GLY164
D	HIS165
D	VAL166
D	TYR167

site_id	CC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO D 1220

Chain	Residue
C	THR76
C	VAL80
D	ASP45
D	ALA47
D	GLY48
D	GLY49
D	HIS57

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 1221

Chain	Residue
C	PRO275
C	ASN301
D	PRO275
D	ASN301

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 1222

Chain	Residue
D	ILE22
D	HIS23
D	PRO24
D	ARG381

site_id	CC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 1223

Chain	Residue
A	ASP45
A	ALA47
A	GLY48
A	GLY49
A	HIS57
B	THR76
B	VAL80
B	LEU81

site_id	CC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO C 1224

Chain	Residue
C	ASP45
C	ALA47
C	GLY48
C	GLY49
C	HIS57
D	THR76
D	VAL80
D	LEU81

site_id	CC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 1225

Chain	Residue
A	GLN69
A	PRO85
B	ALA27
B	ASP28

site_id	CC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 1226

Chain	Residue
C	GLN69
C	LYS72
C	LEU73
C	PRO85
C	HOH1444
D	ASP28
D	HOH1389

site_id	CC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 1227

Chain	Residue
B	TYR167
D	TYR167
D	ARG168
D	HOH1403
D	HOH1465

site_id	DC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 1228

Chain	Residue
A	GLN9
D	LYS96
D	PRO98
D	GLU255

site_id	DC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 1229

Chain	Residue
B	TYR155
B	GLU211
B	ARG398
B	HOH1501
B	HOH1568
B	HOH1570

site_id	DC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 1230

Chain	Residue
C	GLN50
C	GLU211
C	GLN242
C	ARG398
C	HOH1527
D	SO41214
D	HOH1559

site_id	DC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO D 1231

Chain	Residue
D	GLN50
D	GLU211
D	GLN242
D	LYS268
D	ARG398
D	PMP1274
D	HOH1432
D	HOH1560

site_id	DC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1232

Chain	Residue
A	GLN50
A	GLU211
A	GLN242
A	ARG398
A	PMP1271
A	HOH1458

site_id	DC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP A 1261

Chain	Residue
A	GLY111
A	SER112
A	TYR138
A	HIS139
A	GLU206
A	ASP239
A	VAL241
A	GLN242
A	LYS268
A	HOH1273
A	HOH1277
A	HOH1281
A	HOH1351
A	HOH1378
B	THR297
B	HOH1343

site_id	DC7
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP B 1262

Chain	Residue
A	THR297
A	HOH1315
B	THR110
B	GLY111
B	SER112
B	TYR138
B	HIS139
B	GLU206
B	ASP239
B	VAL241
B	GLN242
B	LYS268
B	HOH1273
B	HOH1280
B	HOH1288
B	HOH1318
B	HOH1382

site_id	DC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP C 1263

Chain	Residue
C	GLY111
C	SER112
C	TYR138
C	HIS139
C	GLU206
C	ASP239
C	VAL241
C	GLN242
C	LYS268
C	HOH1287
C	HOH1290
C	HOH1293
C	HOH1306
C	HOH1331
C	HOH1496
D	THR297

site_id	DC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP D 1264

Chain	Residue
C	THR297
C	HOH1291
D	GLY111
D	SER112
D	TYR138
D	HIS139
D	GLU206
D	ASP239
D	VAL241
D	GLN242
D	LYS268
D	HOH1275
D	HOH1285
D	HOH1288
D	HOH1305
D	HOH1311

site_id	EC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PMP A 1271

Chain	Residue
A	GLN50
A	THR110
A	GLY111
A	SER112
A	TYR138
A	HIS139
A	GLU206
A	ASP239
A	VAL241
A	GLN242
A	LYS268
A	EDO1232
A	HOH1273
A	HOH1277
A	HOH1281
A	HOH1351
B	THR297
B	HOH1343

site_id	EC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE PMP B 1272

Chain	Residue
A	THR297
A	HOH1315
B	GLN50
B	THR110
B	GLY111
B	SER112
B	TYR138
B	HIS139
B	GLU206
B	ASP239
B	VAL241
B	GLN242
B	LYS268
B	HOH1273
B	HOH1280
B	HOH1288
B	HOH1318
B	HOH1382
B	HOH1569

site_id	EC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PMP C 1273

Chain	Residue
C	THR110
C	GLY111
C	SER112
C	TYR138
C	HIS139
C	GLU206
C	ASP239
C	VAL241
C	GLN242
C	LYS268
C	HOH1287
C	HOH1290
C	HOH1293
C	HOH1306
C	HOH1331
C	HOH1496
D	THR297
D	HOH1559

site_id	EC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE PMP D 1274

Chain	Residue
C	THR297
C	HOH1291
D	GLN50
D	THR110
D	GLY111
D	SER112
D	TYR138
D	HIS139
D	GLU206
D	ASP239
D	VAL241
D	GLN242
D	LYS268
D	EDO1231
D	HOH1275
D	HOH1285
D	HOH1288
D	HOH1305
D	HOH1311
D	HOH1563

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIaDEVqsgAG.RtGtlfameqmgvap....DLTtfAKsiaGG

Chain	Residue	Details
A	LEU236-GLY273

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15323550","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15723541","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"15323550","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15723541","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SF2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SZS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SZU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	TYR138
A	LYS268
A	ASP239

site_id	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
B	TYR155
B	LYS268
B	ASP239

site_id	CSA11
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
C	TYR155
C	LYS268
C	ASP239

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
D	TYR155
D	LYS268
D	ASP239

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
B	TYR138
B	LYS268
B	ASP239

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
C	TYR138
C	LYS268
C	ASP239

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
D	TYR138
D	LYS268
D	ASP239

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	LYS268
A	HIS139
A	ASP239

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
B	LYS268
B	HIS139
B	ASP239

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
C	LYS268
C	HIS139
C	ASP239

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
D	LYS268
D	HIS139
D	ASP239

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	TYR155
A	LYS268
A	ASP239

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