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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3QPG

Crystal Structures of Escherichia coli Aspartate Aminotransferase Reconstituted with 1-Deaza-Pyridoxal 5'-Phosphate: Internal Aldimine and Stable L-Aspartate External Aldimine

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 aminotransferase 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	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	5
Details	BINDING SITE FOR RESIDUE SO4 A 409

Chain	Residue
A	ARG327
A	GLN328
A	HOH699
A	HOH720
A	HOH732

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 410

Chain	Residue
A	LYS133
A	ARG134
A	ARG372
A	ALA406

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 411

Chain	Residue
A	LYS146
A	ASN150
A	GLU155
A	VAL156
A	ARG157
A	HOH726

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 412

Chain	Residue
A	ALA127
A	VAL132
A	GLY153
A	LEU154
A	HOH568

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 413

Chain	Residue
A	ARG348
A	ASP349

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 414

Chain	Residue
A	LYS49
A	THR55
A	THR74
A	ASN76
A	HOH662

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 415

Chain	Residue
A	PRO84
A	ARG88
A	HOH577
A	HOH690

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 416

Chain	Residue
A	GLY232
A	LEU233
A	GLU234
A	GLU235
A	HOH473
A	HOH618
A	HOH723

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO A 417

Chain	Residue
A	PRO84
A	GLY87
A	ARG88
A	GLN91
A	ARG108
A	THR109
A	HOH489
A	HOH495
A	HOH692

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 418

Chain	Residue
A	HOH6
A	THR90
A	LEU94
A	GLN227
A	SER254
A	TYR256
A	ASN259

site_id	BC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE EDO A 419

Chain	Residue
A	PRO196
A	THR197
A	GLY198
A	ARG334
A	GLN356
A	ASN357
A	GLY358
A	MET359
A	PHE360
A	SER361
A	PHE362
A	HOH485

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 420

Chain	Residue
A	HIS247
A	LYS248
A	GLU249
A	LYS367

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 421

Chain	Residue
A	ARG108
A	HOH670

site_id	BC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 3QP A 422

Chain	Residue
A	HOH11
A	ILE25
A	GLY46
A	TYR77
A	GLY114
A	GLY115
A	THR116
A	TRP142
A	ASN195
A	ASP223
A	TYR226
A	SER255
A	SER257
A	LYS258
A	ARG266
A	ARG292
A	ARG386

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	SER255-GLY268

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	GLY46

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	TRP142

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	ASN195

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	ARG386

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	LYS258

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 777

Chain	Residue	Details
A	TRP142	steric role
A	ASP223	proton shuttle (general acid/base)
A	LYS258	proton shuttle (general acid/base)

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PDB entries from 2024-08-28

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