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5ZCL

Crystal structure of OsPP2C50 I267L:OsPYL/RCAR3 with (+)-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
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG A 401
ChainResidue
AASP118
AASP306
AASP368
AMG402
AHOH502

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 402
ChainResidue
AASP118
AGLY119
AMG401

site_idAC3
Number of Residues13
Detailsbinding site for residue A8S C 301
ChainResidue
CVAL98
CALA104
CPHE125
CHIS130
CPHE174
CLEU178
CLEU179
CASN182
CHOH402
CHOH404
CHOH410
CHOH413
CLYS76

site_idAC4
Number of Residues5
Detailsbinding site for residue MG B 401
ChainResidue
BASP118
BASP306
BASP368
BMG402
BHOH501

site_idAC5
Number of Residues6
Detailsbinding site for residue MG B 402
ChainResidue
BASP118
BGLY119
BMG401
BHOH505
BHOH508
BHOH513

site_idAC6
Number of Residues13
Detailsbinding site for residue A8S D 301
ChainResidue
DLYS76
DVAL98
DALA104
DSER107
DPHE125
DHIS130
DPHE174
DLEU179
DASN182
DHOH402
DHOH404
DHOH405
DHOH407

Functional Information from PROSITE/UniProt
site_idPS01032
Number of Residues9
DetailsPPM_1 PPM-type phosphatase domain signature. LFGVFDGHG
ChainResidueDetails
ALEU113-GLY121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsMotif: {"description":"Modulates binding affinity to PYR/PYL/RCAR abscisic acid intracellular receptors","evidences":[{"source":"PubMed","id":"28827170","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues302
DetailsRegion: {"description":"START-like","evidences":[{"source":"UniProtKB","id":"Q8H1R0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsMotif: {"description":"Gate loop","evidences":[{"source":"UniProtKB","id":"Q8VZS8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsMotif: {"description":"Latch loop","evidences":[{"source":"UniProtKB","id":"Q8VZS8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28827170","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5GWP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O49686","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsSite: {"description":"Involved in ABA binding","evidences":[{"source":"UniProtKB","id":"Q84MC7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsSite: {"description":"Involved in interactions with PP2Cs","evidences":[{"source":"UniProtKB","id":"O49686","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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