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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2QB3

Structural Studies Reveal the Inactivation of E. coli L-Aspartate Aminotransferase by (s)-4,5-dihydro-2-thiophenecarboxylic acid (SADTA) via Two Mechanisms (at pH 7.5)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
A	0004838	molecular_function	L-tyrosine-2-oxoglutarate transaminase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006520	biological_process	amino acid metabolic process
A	0008483	molecular_function	transaminase activity
A	0009058	biological_process	biosynthetic process
A	0009094	biological_process	L-phenylalanine biosynthetic process
A	0016740	molecular_function	transferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0033585	biological_process	L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 801

Chain	Residue
A	PRO72
A	ARG76
A	HOH887

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 802

Chain	Residue
A	LYS134
A	ASN138
A	GLU143
A	VAL144
A	ARG145

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PSZ A 600

Chain	Residue
A	GLY34
A	TYR65
A	GLY103
A	THR104
A	TRP130
A	ASN183
A	ASP211
A	TYR214
A	SER243
A	SER245
A	KST246
A	ARG254
A	PHE348
A	ARG374
A	GOL707
A	HOH808
A	HOH967
A	ILE33

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PMP A 700

Chain	Residue
A	TYR65
A	GLY103
A	THR104
A	TRP130
A	ASN183
A	ASP211
A	TYR214
A	SER243
A	SER245
A	KST246
A	ARG254
A	HOH808

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 701

Chain	Residue
A	GLY216
A	GLY220
A	LEU221
A	GLU308
A	LEU311
A	THR312
A	ARG315
A	HOH1081

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 702

Chain	Residue
A	TYR36
A	THR43
A	PRO44
A	LEU46
A	KST246
A	GLY249
A	TYR251
A	MET314
A	HOH978

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL A 703

Chain	Residue
A	PRO72
A	GLY75
A	ARG76
A	GLN79
A	ALA95
A	ARG96
A	THR97
A	HOH803
A	HOH873
A	HOH1099
A	HOH1154

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 704

Chain	Residue
A	ARG315
A	GLN316
A	GLN319
A	HOH964

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 705

Chain	Residue
A	TYR55
A	THR296
A	ASN300
A	HOH958
A	HOH1060
A	HOH1115
A	HOH1201

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 706

Chain	Residue
A	GLY41
A	THR381
A	HOH984
A	HOH1052
A	HOH1148
A	HOH1204

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 707

Chain	Residue
A	ILE33
A	TYR65
A	KST246
A	ARG280
A	ASN285
A	PSZ600
A	HOH808
A	HOH863
A	HOH1022

Functional Information from PROSITE/UniProt

site_id	PS00105
Number of Residues	14
Details	AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYSKnfGLyNERVG

Chain	Residue	Details
A	SER243-GLY256

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744\|PDB:1ART, ECO:0007744\|PDB:1CZE, ECO:0007744\|PDB:3QPG, ECO:0007744\|PDB:4DBC

Chain	Residue	Details
A	GLY34

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744\|PDB:1AIB, ECO:0007744\|PDB:1ART, ECO:0007744\|PDB:1CZE, ECO:0007744\|PDB:1SPA, ECO:0007744\|PDB:3QPG, ECO:0007744\|PDB:4DBC

Chain	Residue	Details
A	TRP130

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744\|PDB:1AIB, ECO:0007744\|PDB:1ART, ECO:0007744\|PDB:1ASC, ECO:0007744\|PDB:1CZE, ECO:0007744\|PDB:1SPA, ECO:0007744\|PDB:3QPG, ECO:0007744\|PDB:4DBC

Chain	Residue	Details
A	ASN183

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744\|PDB:1AHG, ECO:0007744\|PDB:1AIB, ECO:0007744\|PDB:1ARG, ECO:0007744\|PDB:1ART, ECO:0007744\|PDB:1CZE, ECO:0007744\|PDB:3QPG, ECO:0007744\|PDB:4DBC

Chain	Residue	Details
A	ARG374

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269\|PubMed:11148029, ECO:0000269\|PubMed:1993208, ECO:0000269\|PubMed:3298240, ECO:0000269\|PubMed:9891001, ECO:0007744\|PDB:1AAW, ECO:0007744\|PDB:1AHE, ECO:0007744\|PDB:1AHF, ECO:0007744\|PDB:1AHX, ECO:0007744\|PDB:1AHY, ECO:0007744\|PDB:1ARI, ECO:0007744\|PDB:1ARS, ECO:0007744\|PDB:1ASA, ECO:0007744\|PDB:1ASB, ECO:0007744\|PDB:1ASD, ECO:0007744\|PDB:1ASE, ECO:0007744\|PDB:1ASF, ECO:0007744\|PDB:1ASG, ECO:0007744\|PDB:1ASM, ECO:0007744\|PDB:1ASN, ECO:0007744\|PDB:1B4X, ECO:0007744\|PDB:1CZC, ECO:0007744\|PDB:1CZE, ECO:0007744\|PDB:1G4V, ECO:0007744\|PDB:1G4X, ECO:0007744\|PDB:1G7W, ECO:0007744\|PDB:1G7X, ECO:0007744\|PDB:1IX6, ECO:0007744\|PDB:1IX7, ECO:0007744\|PDB:1IX8, ECO:0007744\|PDB:1QIR, ECO:0007744\|PDB:1QIS, ECO:0007744\|PDB:1QIT, ECO:0007744\|PDB:1YOO, ECO:0007744\|PDB:2D5Y, ECO:0007744\|PDB:2D61, ECO:0007744\|PDB:2D63, ECO:0007744\|PDB:2D7Y, ECO:0007744\|PDB:3AAT, ECO:0007744\|PDB:3ZZJ, ECO:0007744\|PDB:5EAA

Chain	Residue	Details
A	KST246

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	ASP211
A	TRP130

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

Chain	Residue	Details
A	ILE68

site_id	MCSA1
Number of Residues	3
Details	M-CSA 777

Chain	Residue	Details
A	TRP130	steric role
A	ASP211	proton shuttle (general acid/base)
A	KST246	proton shuttle (general acid/base)

237735

PDB entries from 2025-06-18

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