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3KB3

Crystal structure of abscisic acid-bound PYL2 in complex with HAB1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004864molecular_functionprotein phosphatase inhibitor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0009738biological_processabscisic acid-activated signaling pathway
A0010427molecular_functionabscisic acid binding
A0016020cellular_componentmembrane
A0038023molecular_functionsignaling receptor activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0062049cellular_componentprotein phosphatase inhibitor complex
B0004722molecular_functionprotein serine/threonine phosphatase activity
B0006470biological_processprotein dephosphorylation
B0043169molecular_functioncation binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE A8S A 189
ChainResidue
AHOH2
ALEU121
ATYR124
APHE165
AASN173
AHOH204
AHOH209
AHOH217
AHOH3
ALYS64
APHE66
AVAL87
AALA93
ASER96
APHE112
AHIS119

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 997
ChainResidue
BHOH33
BHOH120
BASP243
BASP432
BASP492

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 998
ChainResidue
BGLU203
BASP204
BASP243
BGLY244
BASN493

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 999
ChainResidue
BASP243
BASP346
BSER347
BSER431
BASP432

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 Residues154
DetailsRegion: {"description":"START-like"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsMotif: {"description":"Gate loop","evidences":[{"source":"PubMed","id":"19898420","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsMotif: {"description":"Latch loop","evidences":[{"source":"PubMed","id":"19898420","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues13
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19893533","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19898420","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Involved in interactions with PP2Cs","evidences":[{"source":"UniProtKB","id":"O49686","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Involved in ABA binding","evidences":[{"source":"UniProtKB","id":"Q84MC7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21658606","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3NMT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QN1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UJG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZVU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LA7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LG5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LGA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4WVO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19898420","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3KB3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsSite: {"description":"Lock"}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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