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7DLW

Crystal structure of Arabidopsis ACS7 in complex with PPG

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0009058biological_processbiosynthetic process
A0009693biological_processethylene biosynthetic process
A0009835biological_processfruit ripening
A0016829molecular_functionlyase activity
A0016847molecular_function1-aminocyclopropane-1-carboxylate synthase activity
A0030170molecular_functionpyridoxal phosphate binding
A0042218biological_process1-aminocyclopropane-1-carboxylate biosynthetic process
A0042802molecular_functionidentical protein binding
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0009058biological_processbiosynthetic process
B0009693biological_processethylene biosynthetic process
B0009835biological_processfruit ripening
B0016829molecular_functionlyase activity
B0016847molecular_function1-aminocyclopropane-1-carboxylate synthase activity
B0030170molecular_functionpyridoxal phosphate binding
B0042218biological_process1-aminocyclopropane-1-carboxylate biosynthetic process
B0042802molecular_functionidentical protein binding
C0003824molecular_functioncatalytic activity
C0005515molecular_functionprotein binding
C0009058biological_processbiosynthetic process
C0009693biological_processethylene biosynthetic process
C0009835biological_processfruit ripening
C0016829molecular_functionlyase activity
C0016847molecular_function1-aminocyclopropane-1-carboxylate synthase activity
C0030170molecular_functionpyridoxal phosphate binding
C0042218biological_process1-aminocyclopropane-1-carboxylate biosynthetic process
C0042802molecular_functionidentical protein binding
D0003824molecular_functioncatalytic activity
D0005515molecular_functionprotein binding
D0009058biological_processbiosynthetic process
D0009693biological_processethylene biosynthetic process
D0009835biological_processfruit ripening
D0016829molecular_functionlyase activity
D0016847molecular_function1-aminocyclopropane-1-carboxylate synthase activity
D0030170molecular_functionpyridoxal phosphate binding
D0042218biological_process1-aminocyclopropane-1-carboxylate biosynthetic process
D0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue PPG A 1001
ChainResidue
ATYR33
AASP245
AILE247
ATYR248
ASER282
ASER284
ALYS285
AARG293
AARG419
AHOH1132
ATRP37
ALEU59
AALA60
AGLY134
AALA135
ATHR136
ATYR160
AASN217

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 1002
ChainResidue
AHOH1117
DASP125
DASP127

site_idAC3
Number of Residues17
Detailsbinding site for residue PPG B 1001
ChainResidue
AGLN98
AHOH1165
BTYR33
BALA60
BGLY134
BALA135
BTHR136
BTYR160
BASN217
BASP245
BILE247
BTYR248
BSER282
BSER284
BLYS285
BARG293
BARG419

site_idAC4
Number of Residues18
Detailsbinding site for residue PPG C 1001
ChainResidue
CTYR33
CLEU59
CALA60
CGLY134
CALA135
CTHR136
CTYR160
CASN217
CASP245
CILE247
CTYR248
CSER282
CSER284
CLYS285
CARG293
CARG419
CHOH1102
DGLN98

site_idAC5
Number of Residues15
Detailsbinding site for residue PPG D 1001
ChainResidue
CGLN98
DTYR33
DALA60
DALA135
DTHR136
DTYR160
DASN217
DASP245
DILE247
DTYR248
DSER282
DSER284
DLYS285
DARG293
DARG419

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SLSKdlGLpGFRVG
ChainResidueDetails
ASER282-GLY295

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLU61
ATYR100
BGLU61
BTYR100
CGLU61
CTYR100
DGLU61
DTYR100

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
ALYS285
BLYS285
CLYS285
DLYS285

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PDB entries from 2024-10-09

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