Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1SZK

The structure of gamma-aminobutyrate aminotransferase mutant: E211S

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 701

Chain	Residue
A	ILE184
A	ARG224
A	HOH950

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 702

Chain	Residue
B	LYS5
B	ARG381
B	HOH926

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 703

Chain	Residue
B	HIS188
B	ARG224
B	HOH925

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 704

Chain	Residue
C	HIS188
C	ARG224

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 D 705

Chain	Residue
D	ARG224

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 706

Chain	Residue
D	LYS5
D	ARG381
D	HOH881

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 707

Chain	Residue
A	ASN153
A	TYR394
C	LYS192
C	HOH852

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 708

Chain	Residue
B	ASN153
B	TYR394
D	LYS192

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 709

Chain	Residue
B	LYS192
D	ASN153
D	TYR394

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 710

Chain	Residue
A	LYS192
C	ASN153
C	TYR394

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 711

Chain	Residue
A	GLN419
D	ARG29
D	HOH978

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 712

Chain	Residue
A	ILE50
A	TYR138
A	SER211
A	ARG398
A	PMP750
A	HOH991

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 713

Chain	Residue
B	ILE50
B	TYR138
B	SER211
B	GLN242
B	LYS268
B	ARG398
B	PMP751

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 714

Chain	Residue
C	ILE50
C	TYR138
C	SER211
C	GLN242
C	ARG398
C	PMP752
C	HOH952

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 715

Chain	Residue
D	ILE50
D	TYR138
D	SER211
D	GLN242
D	ARG398
D	PMP753
D	HOH987

site_id	BC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO B 801

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

site_id	BC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO B 802

Chain	Residue
B	HIS23
B	ARG381

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 803

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

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 804

Chain	Residue
B	GLY164
B	HIS165
B	VAL166
D	HIS165
D	VAL166
D	HOH968

site_id	CC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO D 805

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

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 806

Chain	Residue
C	PRO275
C	ASN301
D	PRO275
D	ASN301

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 807

Chain	Residue
D	HIS23
D	PRO24
D	ARG381
D	HOH959

site_id	CC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 808

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

site_id	CC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 809

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

site_id	CC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 810

Chain	Residue
A	GLN69
A	LYS72
A	PRO85
B	ASP28
B	HOH936

site_id	CC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 811

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

site_id	CC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO D 812

Chain	Residue
B	TYR167
D	VAL166
D	TYR167
D	HOH923
D	HOH956
D	HOH968

site_id	DC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 813

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

site_id	DC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PMP A 750

Chain	Residue
A	GLY111
A	SER112
A	TYR138
A	HIS139
A	GLU206
A	ASP239
A	VAL241
A	GLN242
A	LYS268
A	SO4712
A	HOH815
A	HOH823
A	HOH890
A	HOH912
A	HOH987
A	HOH989
B	GLY296
B	THR297

site_id	DC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PMP B 751

Chain	Residue
A	THR297
A	HOH859
B	THR110
B	GLY111
B	SER112
B	TYR138
B	HIS139
B	GLU206
B	ASP239
B	VAL241
B	GLN242
B	LYS268
B	SO4713
B	HOH805
B	HOH811
B	HOH818

site_id	DC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PMP C 752

Chain	Residue
C	THR110
C	GLY111
C	SER112
C	TYR138
C	HIS139
C	GLU206
C	ASP239
C	VAL241
C	GLN242
C	LYS268
C	SO4714
C	HOH825
C	HOH828
C	HOH867
D	THR297
D	HOH838
D	HOH984

site_id	DC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PMP D 753

Chain	Residue
C	THR297
D	GLY111
D	SER112
D	TYR138
D	HIS139
D	GLU206
D	ASP239
D	VAL241
D	GLN242
D	LYS268
D	SO4715
D	HOH813
D	HOH823
D	HOH826
D	HOH836
D	HOH845

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)