1BQA

ASPARTATE AMINOTRANSFERASE P195A MUTANT

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

Functional Information from PDB Data

site_id	ACT
Number of Residues	23
Details	ACTIVE SITE OF SUBUNIT A

Chain	Residue
A	ASP15
A	THR109
A	TRP140
A	ASN194
A	ASP222
A	ALA224
A	TYR225
A	SER255
A	LLP258
A	ARG266
B	ARG292
A	ILE17
B	SER296
B	ASN297
A	PHE360
A	ARG386
A	LEU18
A	ILE37
A	GLY38
A	VAL39
B	TYR70
A	GLY107
A	GLY108

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site_id	BCT
Number of Residues	23
Details	ACTIVE SITE OF SUBUNIT B

Chain	Residue
B	ASP15
B	ILE17
B	LEU18
B	ILE37
B	GLY38
B	VAL39
A	TYR70
B	GLY107
B	GLY108
B	THR109
B	TRP140
B	ASN194
B	ASP222
B	ALA224
B	TYR225
B	SER255
B	LLP258
B	ARG266
A	ARG292
A	SER296
A	ASN297
B	PHE360
B	ARG386

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC

Chain	Residue	Details
A	GLY38
B	GLY38

---

site_id	SWS_FT_FI2
Number of Residues	2
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	TRP140
B	TRP140

---

site_id	SWS_FT_FI3
Number of Residues	2
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	ASN194
B	ASN194

---

site_id	SWS_FT_FI4
Number of Residues	2
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
B	ARG386

---

site_id	SWS_FT_FI5
Number of Residues	2
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	LLP258
B	LLP258

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Catalytic Information from CSA

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

Chain	Residue	Details
A	TRP140
A	ASP222

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
B	TRP140
B	ASP222

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site_id	MCSA1
Number of Residues	3
Details	M-CSA 777

Chain	Residue	Details
A	TRP140	steric role
A	ASP222	proton shuttle (general acid/base)
A	LLP258	proton shuttle (general acid/base)

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site_id	MCSA2
Number of Residues	3
Details	M-CSA 777

Chain	Residue	Details
B	TRP140	steric role
B	ASP222	proton shuttle (general acid/base)
B	LLP258	proton shuttle (general acid/base)

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