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8EY0

Structure of an orthogonal PYR1*:HAB1* chemical-induced dimerization module in complex with mandipropamid

Functional Information from GO Data
ChainGOidnamespacecontents
A0004864molecular_functionprotein phosphatase inhibitor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005773cellular_componentvacuole
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0009705cellular_componentplant-type vacuole membrane
A0009738biological_processabscisic acid-activated signaling pathway
A0010427molecular_functionabscisic acid binding
A0038023molecular_functionsignaling receptor activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0044389molecular_functionubiquitin-like protein ligase binding
A0062049cellular_componentprotein phosphatase inhibitor complex
A0080163biological_processregulation of protein serine/threonine phosphatase activity
A1902584biological_processpositive regulation of response to water deprivation
B0004722molecular_functionprotein serine/threonine phosphatase activity
B0006470biological_processprotein dephosphorylation
B0043169molecular_functioncation binding
Functional Information from PROSITE/UniProt
site_idPS01032
Number of Residues9
DetailsPPM_1 PPM-type phosphatase domain signature. FFGVYDGHG
ChainResidueDetails
BPHE238-GLY246

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:19898494, ECO:0000269|PubMed:19933100
ChainResidueDetails
AARG59
AALA89
AARG116
AGLU141

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Involved in interactions with PP2Cs => ECO:0000269|PubMed:19407142
ChainResidueDetails
APRO88
ASER152

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CARK1 => ECO:0000269|PubMed:29928509
ChainResidueDetails
ATHR78

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PDB entries from 2024-07-24

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