Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4ZSY

Pig Brain GABA-AT inactivated by (Z)-(1S,3S)-3-Amino-4-fluoromethylenyl-1-cyclopentanoic acid.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005829	cellular_component	cytosol
A	0008483	molecular_function	transaminase activity
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	0032144	cellular_component	4-aminobutyrate transaminase complex
A	0032145	molecular_function	succinate-semialdehyde dehydrogenase binding
A	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
A	0047298	molecular_function	(S)-3-amino-2-methylpropionate transaminase activity
A	0050877	biological_process	nervous system process
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0005829	cellular_component	cytosol
B	0008483	molecular_function	transaminase activity
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	0032144	cellular_component	4-aminobutyrate transaminase complex
B	0032145	molecular_function	succinate-semialdehyde dehydrogenase binding
B	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
B	0047298	molecular_function	(S)-3-amino-2-methylpropionate transaminase activity
B	0050877	biological_process	nervous system process
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051537	molecular_function	2 iron, 2 sulfur cluster binding
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0005829	cellular_component	cytosol
C	0008483	molecular_function	transaminase activity
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	0032144	cellular_component	4-aminobutyrate transaminase complex
C	0032145	molecular_function	succinate-semialdehyde dehydrogenase binding
C	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
C	0042802	molecular_function	identical protein binding
C	0042803	molecular_function	protein homodimerization activity
C	0046872	molecular_function	metal ion binding
C	0047298	molecular_function	(S)-3-amino-2-methylpropionate transaminase activity
C	0050877	biological_process	nervous system process
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0005829	cellular_component	cytosol
D	0008483	molecular_function	transaminase activity
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	0032144	cellular_component	4-aminobutyrate transaminase complex
D	0032145	molecular_function	succinate-semialdehyde dehydrogenase binding
D	0034386	molecular_function	4-aminobutyrate:2-oxoglutarate transaminase activity
D	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity
D	0046872	molecular_function	metal ion binding
D	0047298	molecular_function	(S)-3-amino-2-methylpropionate transaminase activity
D	0050877	biological_process	nervous system process
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051537	molecular_function	2 iron, 2 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue FES A 501

Chain	Residue
A	ALA134
A	CYS135
A	CYS138
B	ALA134
B	CYS135
B	CYS138

site_id	AC2
Number of Residues	21
Details	binding site for residue RW2 A 502

Chain	Residue
A	SER137
A	ASN140
A	PHE189
A	HIS190
A	ARG192
A	GLU265
A	GLU270
A	ASP298
A	VAL300
A	GLN301
A	LYS329
A	HOH617
A	HOH634
A	HOH795
A	HOH808
B	PHE351
B	ASN352
B	THR353
A	ILE72
A	CYS135
A	GLY136

site_id	AC3
Number of Residues	8
Details	binding site for residue GOL B 501

Chain	Residue
B	LYS125
B	HIS313
B	GLU314
B	TRP316
B	GLY317
B	LEU318
B	PRO321
B	HOH620

site_id	AC4
Number of Residues	18
Details	binding site for residue RW2 B 502

Chain	Residue
A	PHE351
A	ASN352
A	THR353
B	CYS135
B	GLY136
B	SER137
B	PHE189
B	HIS190
B	ARG192
B	GLU265
B	ASP298
B	VAL300
B	GLN301
B	LYS329
B	HOH611
B	HOH612
B	HOH735
B	HOH824

site_id	AC5
Number of Residues	5
Details	binding site for residue GOL C 501

Chain	Residue
C	ASP278
C	ARG282
C	HIS315
C	HOH717
C	HOH896

site_id	AC6
Number of Residues	22
Details	binding site for residue RW2 C 502

Chain	Residue
C	ILE72
C	CYS135
C	GLY136
C	SER137
C	PHE189
C	HIS190
C	ARG192
C	GLU265
C	GLU270
C	ASP298
C	VAL300
C	GLN301
C	LYS329
C	ARG445
C	HOH628
C	HOH644
C	HOH740
C	HOH804
C	HOH836
D	PHE351
D	ASN352
D	THR353

site_id	AC7
Number of Residues	6
Details	binding site for residue FES D 501

Chain	Residue
C	ALA134
C	CYS135
C	CYS138
D	ALA134
D	CYS135
D	CYS138

site_id	AC8
Number of Residues	21
Details	binding site for residue RW2 D 502

Chain	Residue
D	ASP298
D	VAL300
D	GLN301
D	LYS329
D	HOH611
D	HOH747
D	HOH830
D	HOH869
C	PHE351
C	ASN352
C	THR353
D	ILE72
D	CYS135
D	GLY136
D	SER137
D	ASN140
D	PHE189
D	HIS190
D	ARG192
D	GLU265
D	GLU270

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	40
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FLvDEVqtgGG.StGkfwahehwglddpa..DVMtfSKkmmTG

Chain	Residue	Details
A	PHE295-GLY334

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14534310","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"10393538","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14534310","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10393538","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10393538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14534310","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P61922","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P61922","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	16
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P61922","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"10393538","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 854

Chain	Residue	Details
A	PHE189	steric role
A	ASP298	electrostatic stabiliser
A	LYS329	covalent catalysis, proton shuttle (general acid/base)
A	THR353	electrostatic stabiliser

site_id	MCSA2
Number of Residues	4
Details	M-CSA 854

Chain	Residue	Details
B	PHE189	steric role
B	ASP298	electrostatic stabiliser
B	LYS329	covalent catalysis, proton shuttle (general acid/base)
B	THR353	electrostatic stabiliser

site_id	MCSA3
Number of Residues	4
Details	M-CSA 854

Chain	Residue	Details
C	PHE189	steric role
C	ASP298	electrostatic stabiliser
C	LYS329	covalent catalysis, proton shuttle (general acid/base)
C	THR353	electrostatic stabiliser

site_id	MCSA4
Number of Residues	4
Details	M-CSA 854

Chain	Residue	Details
D	PHE189	steric role
D	ASP298	electrostatic stabiliser
D	LYS329	covalent catalysis, proton shuttle (general acid/base)
D	THR353	electrostatic stabiliser

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