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3PIU

High-resolution structure of native Malus domestica ACC synthase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006520biological_processamino acid metabolic process
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0009693biological_processethylene biosynthetic process
A0009835biological_processfruit ripening
A0016491molecular_functionoxidoreductase activity
A0016829molecular_functionlyase activity
A0016847molecular_function1-aminocyclopropane-1-carboxylate synthase activity
A0030170molecular_functionpyridoxal phosphate binding
A0042218biological_process1-aminocyclopropane-1-carboxylate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLR A 500
ChainResidue
AGLY119
ASER270
ASER272
ALLP273
AARG281
AHOH654
AHOH727
AALA120
ATHR121
ATYR145
ATHR198
AASN202
AASP230
AILE232
ATYR233

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SLSKdlGLpGFRVG
ChainResidueDetails
ASER270-GLY283

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12686108","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1M4N","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12686108","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1B8G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M4N","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"10610793","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9398277","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B8G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PIU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 418
ChainResidueDetails
ATYR145activator, steric role
AASP230electrostatic stabiliser
AILE232steric role
ALLP273covalent catalysis, proton shuttle (general acid/base)

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PDB entries from 2025-12-17

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