Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1SZU

The structure of gamma-aminobutyrate aminotransferase mutant: V241A

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 1001

Chain	Residue
A	ARG224
A	HOH1725
A	HOH1808

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 1002

Chain	Residue
B	LYS5
B	ARG381
B	HOH1710

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 1003

Chain	Residue
B	ILE184
B	HIS188
B	ARG224

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 1004

Chain	Residue
C	HIS188
C	ARG224

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 D 1005

Chain	Residue
D	ILE184
D	ARG224

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 1006

Chain	Residue
B	HOH1725
D	LYS5
D	ARG381

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 1007

Chain	Residue
A	LYS151
A	ASN153
A	TYR394
C	LYS192

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 1008

Chain	Residue
B	ASN153
B	TYR394
D	LYS192

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 1009

Chain	Residue
B	LYS192
D	LYS151
D	TYR394

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 1010

Chain	Residue
A	LYS192
C	ASN153
C	TYR394

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 1011

Chain	Residue
A	GLN419
A	HOH1768
C	LYS71
D	ARG29

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO B 1021

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

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 1022

Chain	Residue
B	HIS23
B	ARG381
B	HOH1820

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 1023

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

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO B 1024

Chain	Residue
B	GLY164
B	HIS165
B	VAL166
B	TYR167
B	HOH1579
D	HIS165
D	VAL166
D	TYR167

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO D 1025

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

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 1026

Chain	Residue
C	PRO275
C	ASN301
D	PRO275
D	ASN301
D	ILE303

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO D 1027

Chain	Residue
D	ILE22
D	HIS23
D	ARG381

site_id	CC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 1028

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

site_id	CC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO C 1029

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

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1030

Chain	Residue
A	GLN69
A	LYS72
A	LEU73
A	PRO85
B	ASP28
B	HOH1747

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 1031

Chain	Residue
C	HOH1658
D	ALA27
D	ASP28
C	GLN69
C	LEU73
C	PRO85

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 1032

Chain	Residue
B	TYR167
B	HOH1745
D	TYR167
D	ARG168
D	HOH1695

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 1033

Chain	Residue
A	GLN9
D	GLN95
D	LYS96
D	PRO98
D	GLU255

site_id	CC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 1034

Chain	Residue
C	GLN79
C	GLY292
C	LEU294
C	HOH1775
D	GLY18
D	GLY20
D	ILE22

site_id	CC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP A 1466

Chain	Residue
A	GLY111
A	SER112
A	TYR138
A	GLU206
A	ASP239
A	ALA241
A	GLN242
A	LYS268
A	HOH1568
A	HOH1572
A	HOH1577
A	HOH1814
B	GLY296
B	THR297
B	HOH1636

site_id	CC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PLP B 1467

Chain	Residue
A	THR297
A	HOH1614
B	THR110
B	GLY111
B	SER112
B	TYR138
B	HIS139
B	GLU206
B	ASP239
B	ALA241
B	GLN242
B	LYS268
B	HOH1574
B	HOH1582
B	HOH1611
B	HOH1814

site_id	DC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP C 1468

Chain	Residue
C	THR110
C	GLY111
C	SER112
C	TYR138
C	HIS139
C	GLU206
C	ASP239
C	ALA241
C	GLN242
C	LYS268
C	HOH1582
C	HOH1585
C	HOH1588
C	HOH1627
D	GLY296
D	THR297
D	HOH1613

site_id	DC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP D 1469

Chain	Residue
C	THR297
C	HOH1586
D	THR110
D	GLY111
D	SER112
D	TYR138
D	HIS139
D	GLU206
D	ASP239
D	ALA241
D	GLN242
D	LYS268
D	HOH1570
D	HOH1580
D	HOH1583
D	HOH1808
D	HOH1811

site_id	DC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PMP A 1566

Chain	Residue
A	THR110
A	GLY111
A	SER112
A	TYR138
A	HIS139
A	GLU206
A	GLU211
A	ASP239
A	ALA241
A	GLN242
A	LYS268
A	HOH1568
A	HOH1572
A	HOH1577
A	HOH1811
A	HOH1814
B	THR297
B	HOH1636

site_id	DC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE PMP B 1567

Chain	Residue
A	THR297
A	HOH1614
B	THR110
B	GLY111
B	SER112
B	TYR138
B	HIS139
B	GLU206
B	GLU211
B	ASP239
B	ALA241
B	GLN242
B	LYS268
B	HOH1574
B	HOH1582
B	HOH1611
B	HOH1616
B	HOH1811
B	HOH1814
B	HOH1817

site_id	DC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PMP C 1568

Chain	Residue
C	THR110
C	GLY111
C	SER112
C	TYR138
C	HIS139
C	GLU206
C	ASP239
C	ALA241
C	GLN242
C	LYS268
C	HOH1582
C	HOH1585
C	HOH1588
C	HOH1627
C	HOH1774
D	THR297
D	HOH1613

site_id	DC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE PMP D 1569

Chain	Residue
C	THR297
C	HOH1586
D	THR110
D	GLY111
D	SER112
D	TYR138
D	HIS139
D	GLU206
D	GLU211
D	ASP239
D	ALA241
D	GLN242
D	LYS268
D	HOH1570
D	HOH1580
D	HOH1583
D	HOH1808
D	HOH1810
D	HOH1811

Functional Information from PROSITE/UniProt

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

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