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3NMV

Crystal structure of pyrabactin-bound abscisic acid receptor PYL2 mutant A93F in complex with type 2C protein phosphatase ABI2

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 Residues12
DetailsBINDING SITE FOR RESIDUE PYV A 900
ChainResidue
AHOH7
AASN173
AHOH217
AHOH267
ALYS64
APHE93
ASER96
AGLU98
APHE112
ATYR124
APHE165
AVAL169

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 424
ChainResidue
BHOH1
BASP127
BASP165
BASP337
BASP402
BASN403

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 425
ChainResidue
BASP165
BASP251
BSER252
BSER336
BASP337

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 426
ChainResidue
BHOH11
BHOH75
BGLU126
BGLY166
BHOH428

Functional Information from PROSITE/UniProt
site_idPS01032
Number of Residues9
DetailsPPM_1 PPM-type phosphatase domain signature. FFGVYDGHG
ChainResidueDetails
BPHE160-GLY168

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":"20729862","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22116026","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3NMV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UJK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UJL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20729862","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22116026","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3NMV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UJL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsSite: {"description":"Lock","evidences":[{"source":"UniProtKB","id":"Q9CAJ0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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