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5ZCU

Crystal structure of RCAR3:PP2C wild-type with pyrabactin

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 Residues6
Detailsbinding site for residue MG A 401
ChainResidue
AASP118
AASP306
AASP368
AHOH509
AHOH518
CHOH412

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 402
ChainResidue
AHOH517
CHOH414
AASP118
AGLY119
AHOH509

site_idAC3
Number of Residues5
Detailsbinding site for residue MG B 401
ChainResidue
BASP118
BASP306
BASP368
BHOH517
BHOH531

site_idAC4
Number of Residues5
Detailsbinding site for residue MG B 402
ChainResidue
BASP75
BASP118
BGLY119
BHOH502
BHOH517

site_idAC5
Number of Residues14
Detailsbinding site for residue PYV C 301
ChainResidue
CLYS76
CPHE78
CVAL79
CPRO103
CSER107
CGLU109
CPHE125
CHIS130
CLEU132
CTYR135
CLEU179
CASN182
CHOH404
CHOH417

site_idAC6
Number of Residues7
Detailsbinding site for residue SO4 C 302
ChainResidue
CSER100
CGLY101
CHOH402
CHOH403
CHOH412
CHOH414
CHOH421

site_idAC7
Number of Residues13
Detailsbinding site for residue PYV D 301
ChainResidue
DLYS76
DPHE78
DVAL79
DPRO103
DSER107
DPHE125
DHIS130
DLEU132
DTYR135
DLEU178
DLEU179
DASN182
DHOH409

site_idAC8
Number of Residues5
Detailsbinding site for residue SO4 D 302
ChainResidue
BASP368
BHOH502
BHOH517
DGLY101
DHOH405

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

246031

PDB entries from 2025-12-10

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