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3NMH

Crystal structure of the abscisic receptor PYL2 in complex with pyrabactin

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
A0038023molecular_functionsignaling receptor activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0062049cellular_componentprotein phosphatase inhibitor complex
B0004864molecular_functionprotein phosphatase inhibitor activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0009738biological_processabscisic acid-activated signaling pathway
B0010427molecular_functionabscisic acid binding
B0038023molecular_functionsignaling receptor activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0062049cellular_componentprotein phosphatase inhibitor complex
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
C0038023molecular_functionsignaling receptor activity
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0062049cellular_componentprotein phosphatase inhibitor complex
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PYV A 900
ChainResidue
ALYS64
AHOH195
AHOH243
BEPE190
AVAL67
AGLU98
APHE112
AGLU118
ATYR124
AVAL166
AVAL169
AASN173

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE EPE A 200
ChainResidue
ASER89
AGLY90
ALEU91
AGLU118
AHIS119
ALEU121
AHOH191
AHOH257
AHOH298
BSER89
BGLY90
BEPE190
BHOH260

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PYV B 900
ChainResidue
BHOH10
BLYS64
BGLU98
BPHE112
BTYR124
BPHE165
BVAL169
BASN173
BEPE190
BHOH276

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE EPE B 190
ChainResidue
APHE66
ASER89
AEPE200
APYV900
BPHE66
BVAL87
BILE88
BSER89
BPHE165
BHOH260
BPYV900

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PYV C 900
ChainResidue
CLYS64
CVAL87
CGLU98
CPHE112
CGLU118
CTYR124
CPHE165
CVAL169
CASN173
CHOH225
CHOH227

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues462
DetailsRegion: {"description":"START-like"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsMotif: {"description":"Gate loop","evidences":[{"source":"PubMed","id":"19898420","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsMotif: {"description":"Latch loop","evidences":[{"source":"PubMed","id":"19898420","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues39
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19893533","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19898420","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsSite: {"description":"Involved in interactions with PP2Cs","evidences":[{"source":"UniProtKB","id":"O49686","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsSite: {"description":"Involved in ABA binding","evidences":[{"source":"UniProtKB","id":"Q84MC7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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