3PIU

High-resolution structure of native Malus domestica ACC synthase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
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	0016491	molecular_function	oxidoreductase activity
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLR A 500

Chain	Residue
A	GLY119
A	SER270
A	SER272
A	LLP273
A	ARG281
A	HOH654
A	HOH727
A	ALA120
A	THR121
A	TYR145
A	THR198
A	ASN202
A	ASP230
A	ILE232
A	TYR233

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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	SER270-GLY283

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305|PubMed:12686108, ECO:0007744|PDB:1M4N

Chain	Residue	Details
A	ASP84

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:12686108, ECO:0007744|PDB:1B8G, ECO:0007744|PDB:1M4N

Chain	Residue	Details
A	TYR145
A	ASP151

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10610793, ECO:0000269|PubMed:9398277, ECO:0007744|PDB:1B8G, ECO:0007744|PDB:3PIU

Chain	Residue	Details
A	LLP273

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 418

Chain	Residue	Details
A	TYR145	activator, steric role
A	ASP230	electrostatic stabiliser
A	ILE232	steric role
A	LLP273	covalent catalysis, proton shuttle (general acid/base)

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