7DLY

Crystal structure of Arabidopsis ACS7 mutant in complex with PPG

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0006520	biological_process	amino acid metabolic process
A	0008483	molecular_function	transaminase activity
A	0009058	biological_process	biosynthetic process
A	0009693	biological_process	ethylene biosynthetic process
A	0009835	biological_process	fruit ripening
A	0016829	molecular_function	lyase activity
A	0016847	molecular_function	1-aminocyclopropane-1-carboxylate synthase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042218	biological_process	1-aminocyclopropane-1-carboxylate biosynthetic process
A	0042802	molecular_function	identical protein binding
B	0003824	molecular_function	catalytic activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0006520	biological_process	amino acid metabolic process
B	0008483	molecular_function	transaminase activity
B	0009058	biological_process	biosynthetic process
B	0009693	biological_process	ethylene biosynthetic process
B	0009835	biological_process	fruit ripening
B	0016829	molecular_function	lyase activity
B	0016847	molecular_function	1-aminocyclopropane-1-carboxylate synthase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0042218	biological_process	1-aminocyclopropane-1-carboxylate biosynthetic process
B	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue PPG A 1001

Chain	Residue
A	TYR33
A	ASN217
A	ASP245
A	ILE247
A	TYR248
A	SER282
A	SER284
A	LYS285
A	ARG293
A	ARG419
A	LEU59
A	ALA60
A	GLU61
A	GLY134
A	ALA135
A	THR136
A	TYR160
A	THR213

---

site_id	AC2
Number of Residues	16
Details	binding site for residue PPG B 1001

Chain	Residue
B	TYR33
B	ALA60
B	GLU61
B	ALA135
B	THR136
B	TYR160
B	THR213
B	ASN217
B	ASP245
B	ILE247
B	TYR248
B	SER282
B	SER284
B	LYS285
B	ARG293
B	ARG419

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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. SLSKdlGLpGFRVG

Chain	Residue	Details
A	SER282-GLY295

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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