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5GJ9

Crystal structure of Arabidopsis thaliana ACO2 in complex with POA

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0005634cellular_componentnucleus
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006952biological_processdefense response
A0009505cellular_componentplant-type cell wall
A0009506cellular_componentplasmodesma
A0009693biological_processethylene biosynthetic process
A0009727biological_processdetection of ethylene stimulus
A0009815molecular_function1-aminocyclopropane-1-carboxylate oxidase activity
A0010030biological_processpositive regulation of seed germination
A0016491molecular_functionoxidoreductase activity
A0031418molecular_functionL-ascorbic acid binding
A0046872molecular_functionmetal ion binding
A0071398biological_processcellular response to fatty acid
A0071732biological_processcellular response to nitric oxide
B0005507molecular_functioncopper ion binding
B0005634cellular_componentnucleus
B0005783cellular_componentendoplasmic reticulum
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006952biological_processdefense response
B0009505cellular_componentplant-type cell wall
B0009506cellular_componentplasmodesma
B0009693biological_processethylene biosynthetic process
B0009727biological_processdetection of ethylene stimulus
B0009815molecular_function1-aminocyclopropane-1-carboxylate oxidase activity
B0010030biological_processpositive regulation of seed germination
B0016491molecular_functionoxidoreductase activity
B0031418molecular_functionL-ascorbic acid binding
B0046872molecular_functionmetal ion binding
B0071398biological_processcellular response to fatty acid
B0071732biological_processcellular response to nitric oxide
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS180
AASP182
AHIS237
AVGL402

site_idAC2
Number of Residues10
Detailsbinding site for residue VGL A 402
ChainResidue
AASN219
AHIS237
AALA251
AZN401
AHOH518
ALYS161
ALEU177
AHIS180
AASP182
ALEU189

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BHIS180
BASP182
BHIS237
BVGL402

site_idAC4
Number of Residues9
Detailsbinding site for residue VGL B 402
ChainResidue
BLYS161
BLEU177
BHIS180
BASP182
BASN219
BHIS237
BALA251
BZN401
BHOH509

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00805
ChainResidueDetails
AHIS180
AASP182
AHIS237
AARG247
BHIS180
BASP182
BHIS237
BARG247

226707

PDB entries from 2024-10-30

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