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3NJ0

X-ray crystal structure of the PYL2-pyrabactin A complex

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 Residues13
DetailsBINDING SITE FOR RESIDUE PYV A 300
ChainResidue
ALYS64
APEG191
AHOH214
AHOH284
AHOH285
AGLU98
APHE112
AVAL114
ALEU121
ATYR124
APHE165
AVAL169
AASN173

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 191
ChainResidue
APHE66
APYV300
BSER89
BPHE165
BPYV300

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PYV B 300
ChainResidue
APEG191
BLYS64
BVAL87
BGLU98
BPHE112
BVAL114
BLEU121
BTYR124
BPHE165
BVAL169
BASN173
BHOH209
BHOH229

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PYV C 300
ChainResidue
CLYS64
CVAL87
CGLU98
CPHE112
CVAL114
CLEU121
CTYR124
CPHE165
CVAL166
CVAL169
CPEG191
CGOL192
CHOH278
CHOH279
CHOH291

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG C 191
ChainResidue
CPHE66
CPHE165
CPHE165
CGOL192
CPYV300

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 192
ChainResidue
CGLY90
CHIS119
CARG120
CLEU121
CPEG191
CPYV300

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:19893533, ECO:0000269|PubMed:19898420
ChainResidueDetails
ALYS64
CALA93
CARG120
CGLU147
AALA93
AARG120
AGLU147
BLYS64
BALA93
BARG120
BGLU147
CLYS64

site_idSWS_FT_FI2
Number of Residues6
DetailsSITE: Involved in interactions with PP2Cs => ECO:0000250|UniProtKB:O49686
ChainResidueDetails
APRO92
ATHR158
BPRO92
BTHR158
CPRO92
CTHR158

site_idSWS_FT_FI3
Number of Residues3
DetailsSITE: Involved in ABA binding => ECO:0000250|UniProtKB:Q84MC7
ChainResidueDetails
AVAL166
BVAL166
CVAL166

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PDB entries from 2024-10-30

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