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1B8G

1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
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
B0003824molecular_functioncatalytic activity
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0009693biological_processethylene biosynthetic process
B0009835biological_processfruit ripening
B0016491molecular_functionoxidoreductase activity
B0016829molecular_functionlyase activity
B0016847molecular_function1-aminocyclopropane-1-carboxylate synthase activity
B0030170molecular_functionpyridoxal phosphate binding
B0042218biological_process1-aminocyclopropane-1-carboxylate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP A 500
ChainResidue
AGLY119
AALA120
ATHR121
ATYR145
AASN202
AASP230
AILE232
ATYR233
ASER270
ASER272
ALYS273
AARG281
AHOH521

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PLP B 500
ChainResidue
BGLY119
BALA120
BTHR121
BTYR145
BASN202
BILE232
BTYR233
BSER270
BSER272
BLYS273
BARG281
BHOH527

site_idACT
Number of Residues9
DetailsIN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT
ChainResidue
BTYR85
ATHR121
AASN202
AASP230
ATYR233
ASER270
ALYS273
AARG281
AARG407

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 Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:12686108, ECO:0007744|PDB:1M4N
ChainResidueDetails
AASP84
BASP84

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:12686108, ECO:0007744|PDB:1B8G, ECO:0007744|PDB:1M4N
ChainResidueDetails
ATYR145
AASP151
BTYR145
BASP151

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10610793, ECO:0000269|PubMed:9398277, ECO:0007744|PDB:1B8G, ECO:0007744|PDB:3PIU
ChainResidueDetails
ALYS273
BLYS273

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 418
ChainResidueDetails
ATYR145activator, steric role
AASP230electrostatic stabiliser
AILE232steric role
ALYS273covalent catalysis, proton shuttle (general acid/base)

site_idMCSA2
Number of Residues4
DetailsM-CSA 418
ChainResidueDetails
BTYR145activator, steric role
BASP230electrostatic stabiliser
BILE232steric role
BLYS273covalent catalysis, proton shuttle (general acid/base)

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PDB entries from 2024-04-24

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