Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5VWQ

E.coli Aspartate aminotransferase-(1R,3S,4S)-3-amino-4-fluorocyclopentane-1-carboxylic acid (FCP)

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	0006533	biological_process	aspartate catabolic 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
D	0003824	molecular_function	catalytic activity
D	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
D	0004838	molecular_function	L-tyrosine:2-oxoglutarate aminotransferase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006520	biological_process	amino acid metabolic process
D	0006533	biological_process	aspartate catabolic process
D	0008483	molecular_function	transaminase activity
D	0009058	biological_process	biosynthetic process
D	0009094	biological_process	L-phenylalanine biosynthetic process
D	0016740	molecular_function	transferase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0033585	biological_process	L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
D	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity
G	0003824	molecular_function	catalytic activity
G	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
G	0004838	molecular_function	L-tyrosine:2-oxoglutarate aminotransferase activity
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0006520	biological_process	amino acid metabolic process
G	0006533	biological_process	aspartate catabolic process
G	0008483	molecular_function	transaminase activity
G	0009058	biological_process	biosynthetic process
G	0009094	biological_process	L-phenylalanine biosynthetic process
G	0016740	molecular_function	transferase activity
G	0030170	molecular_function	pyridoxal phosphate binding
G	0033585	biological_process	L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
G	0042802	molecular_function	identical protein binding
G	0042803	molecular_function	protein homodimerization activity
J	0003824	molecular_function	catalytic activity
J	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
J	0004838	molecular_function	L-tyrosine:2-oxoglutarate aminotransferase activity
J	0005737	cellular_component	cytoplasm
J	0005829	cellular_component	cytosol
J	0006520	biological_process	amino acid metabolic process
J	0006533	biological_process	aspartate catabolic process
J	0008483	molecular_function	transaminase activity
J	0009058	biological_process	biosynthetic process
J	0009094	biological_process	L-phenylalanine biosynthetic process
J	0016740	molecular_function	transferase activity
J	0030170	molecular_function	pyridoxal phosphate binding
J	0033585	biological_process	L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
J	0042802	molecular_function	identical protein binding
J	0042803	molecular_function	protein homodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue PMP A 401

Chain	Residue
A	GLY103
A	ARG254
A	HOH681
D	TYR65
A	THR104
A	TRP130
A	ASN183
A	ASP211
A	TYR214
A	SER243
A	SER245
A	LYS246

site_id	AC2
Number of Residues	12
Details	binding site for residue PMP D 401

Chain	Residue
A	TYR65
D	GLY103
D	THR104
D	TRP130
D	ASN183
D	ASP211
D	TYR214
D	SER243
D	SER245
D	LYS246
D	ARG254
D	HOH669

site_id	AC3
Number of Residues	13
Details	binding site for residue PMP G 401

Chain	Residue
G	GLY102
G	GLY103
G	THR104
G	TRP130
G	ASN183
G	ASP211
G	TYR214
G	SER243
G	SER245
G	LYS246
G	ARG254
J	TYR65
J	HOH683

site_id	AC4
Number of Residues	13
Details	binding site for residue PMP J 401

Chain	Residue
G	TYR65
J	GLY102
J	GLY103
J	THR104
J	TRP130
J	ASN183
J	ASP211
J	TYR214
J	SER243
J	SER245
J	LYS246
J	ARG254
J	HOH600

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	4
Details	BINDING: BINDING => ECO:0007744\|PDB:1ART, ECO:0007744\|PDB:1CZE, ECO:0007744\|PDB:3QPG, ECO:0007744\|PDB:4DBC

Chain	Residue	Details
A	GLY34
D	GLY34
G	GLY34
J	GLY34

site_id	SWS_FT_FI2
Number of Residues	4
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
D	TRP130
G	TRP130
J	TRP130
A	TRP130

site_id	SWS_FT_FI3
Number of Residues	4
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
D	ASN183
G	ASN183
J	ASN183

site_id	SWS_FT_FI4
Number of Residues	4
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
D	ARG374
G	ARG374
J	ARG374

site_id	SWS_FT_FI5
Number of Residues	4
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	LYS246
D	LYS246
G	LYS246
J	LYS246

Catalytic Information from CSA

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	LYS246	proton shuttle (general acid/base)

site_id	MCSA2
Number of Residues	3
Details	M-CSA 777

Chain	Residue	Details
D	TRP130	steric role
D	ASP211	proton shuttle (general acid/base)
D	LYS246	proton shuttle (general acid/base)

site_id	MCSA3
Number of Residues	3
Details	M-CSA 777

Chain	Residue	Details
G	TRP130	steric role
G	ASP211	proton shuttle (general acid/base)
G	LYS246	proton shuttle (general acid/base)

site_id	MCSA4
Number of Residues	3
Details	M-CSA 777

Chain	Residue	Details
J	TRP130	steric role
J	ASP211	proton shuttle (general acid/base)
J	LYS246	proton shuttle (general acid/base)

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