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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2QA3

Structural Studies Reveal the Inactivation of E. coli L-aspartate aminotransferase by (S)-4,5-amino-dihydro-2-thiophenecarboxylic acid (SADTA) via two mechanisms (at pH6.5)

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 601

Chain	Residue
A	PRO72
A	ARG76
A	HOH784

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 602

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

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 603

Chain	Residue
A	ARG315
A	GOL501
A	GOL504
A	GOL508
A	HOH823
A	HOH940
A	HOH943
A	HOH1010
A	THR312

site_id	AC4
Number of Residues	17
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	GOL511
A	HOH706
A	HOH853

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PMP A 700

Chain	Residue
A	TYR65
A	GLY102
A	GLY103
A	THR104
A	TRP130
A	ASN183
A	ASP211
A	TYR214
A	SER243
A	SER245
A	KST246
A	ARG254
A	HOH706

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL A 501

Chain	Residue
A	GLY216
A	GLY220
A	LEU221
A	GLU308
A	LEU311
A	THR312
A	ARG315
A	GOL508
A	SO4603
A	HOH943
A	HOH1075

site_id	AC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE GOL A 502

Chain	Residue
A	TYR36
A	THR43
A	PRO44
A	LEU46
A	KST246
A	GLY249
A	TYR251
A	GLU310
A	ASP313
A	MET314
A	HOH741
A	HOH855
A	HOH901

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 503

Chain	Residue
A	PRO72
A	GLY75
A	ARG76
A	GLN79
A	ALA95
A	ARG96
A	THR97
A	HOH701
A	HOH744
A	HOH955

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 504

Chain	Residue
A	ALA218
A	ARG315
A	GLN316
A	GLN319
A	SO4603
A	HOH767
A	HOH851
A	HOH911
A	HOH1000

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 505

Chain	Residue
A	HOH1042
A	GLU3
A	ASN4
A	TYR150
A	PHE350
A	SER372
A	HOH735
A	HOH987
A	HOH1003
A	HOH1016

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 506

Chain	Residue
A	TYR55
A	ASN300
A	LEU303
A	HOH845
A	HOH965

site_id	BC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GOL A 507

Chain	Residue
A	PRO189
A	THR190
A	LEU191
A	ARG219
A	ASN345
A	HOH724
A	HOH747
A	HOH792
A	HOH804
A	HOH875
A	HOH953
A	HOH1009

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 508

Chain	Residue
A	GLY220
A	LEU221
A	GLU222
A	GLU223
A	GOL501
A	SO4603
A	HOH940
A	HOH1075

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 509

Chain	Residue
A	GLY41
A	THR381
A	ASN384
A	HOH866
A	HOH1051
A	HOH1052

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 510

Chain	Residue
A	ASP301
A	ALA302
A	ARG304
A	ALA305
A	GLU308
A	HOH760
A	HOH923
A	HOH1081

site_id	BC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 511

Chain	Residue
A	ILE33
A	TYR65
A	KST246
A	ARG280
A	ASN285
A	PSZ600
A	HOH706
A	HOH761
A	HOH896
A	HOH1033

site_id	BC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 512

Chain	Residue
A	ASN30
A	LEU31
A	GLY32
A	ILE33
A	GLY34
A	VAL35
A	ASN376
A	HOH1011

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 513

Chain	Residue
A	GLY67
A	ILE68
A	ASP69
A	LYS276
A	HOH761
A	HOH840

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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