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3RT0

Crystal structure of PYL10-HAB1 complex in the absence of abscisic acid (ABA)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004722molecular_functionprotein serine/threonine phosphatase activity
A0006470biological_processprotein dephosphorylation
A0043169molecular_functioncation binding
B0004722molecular_functionprotein serine/threonine phosphatase activity
B0006470biological_processprotein dephosphorylation
B0043169molecular_functioncation binding
C0004864molecular_functionprotein phosphatase inhibitor activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005886cellular_componentplasma membrane
C0009738biological_processabscisic acid-activated signaling pathway
C0010427molecular_functionabscisic acid binding
C0016020cellular_componentmembrane
C0038023molecular_functionsignaling receptor activity
C0042803molecular_functionprotein homodimerization activity
C0080163biological_processregulation of protein serine/threonine phosphatase activity
D0004864molecular_functionprotein phosphatase inhibitor activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005886cellular_componentplasma membrane
D0009738biological_processabscisic acid-activated signaling pathway
D0010427molecular_functionabscisic acid binding
D0016020cellular_componentmembrane
D0038023molecular_functionsignaling receptor activity
D0042803molecular_functionprotein homodimerization activity
D0080163biological_processregulation of protein serine/threonine phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 512
ChainResidue
AASP243
AASP432
AASP492
AHOH544
AHOH681
AHOH727

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 512
ChainResidue
BHOH673
BHOH674
BHOH675
BASP243
BASP432
BASP492

Functional Information from PROSITE/UniProt
site_idPS01032
Number of Residues9
DetailsPPM_1 PPM-type phosphatase domain signature. FFGVYDGHG
ChainResidueDetails
APHE238-GLY246

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|Ref.10, ECO:0007744|PDB:3R6P
ChainResidueDetails
CLYS56
DLYS56
AASP492
BASP243
BASP432
BASP492

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O49686
ChainResidueDetails
CALA85
CARG112
CGLU137
DALA85
DARG112
DGLU137

site_idSWS_FT_FI3
Number of Residues8
DetailsSITE: Involved in ABA binding => ECO:0000250|UniProtKB:Q84MC7
ChainResidueDetails
CPRO57
CILE104
CVAL156
CLEU159
DPRO57
DILE104
DVAL156
DLEU159

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Involved in interactions with PP2Cs => ECO:0000250|UniProtKB:O49686
ChainResidueDetails
CPRO84
CTHR148
DPRO84
DTHR148

218853

PDB entries from 2024-04-24

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