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3NJO

X-ray crystal structure of the Pyr1-pyrabactin A complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004864molecular_functionprotein phosphatase inhibitor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005773cellular_componentvacuole
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0009705cellular_componentplant-type vacuole membrane
A0009738biological_processabscisic acid-activated signaling pathway
A0010427molecular_functionabscisic acid binding
A0038023molecular_functionsignaling receptor activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0044389molecular_functionubiquitin-like protein ligase binding
A0062049cellular_componentprotein phosphatase inhibitor complex
A0080163biological_processregulation of protein serine/threonine phosphatase activity
A1902584biological_processpositive regulation of response to water deprivation
B0004864molecular_functionprotein phosphatase inhibitor activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005773cellular_componentvacuole
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0009705cellular_componentplant-type vacuole membrane
B0009738biological_processabscisic acid-activated signaling pathway
B0010427molecular_functionabscisic acid binding
B0038023molecular_functionsignaling receptor activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0044389molecular_functionubiquitin-like protein ligase binding
B0062049cellular_componentprotein phosphatase inhibitor complex
B0080163biological_processregulation of protein serine/threonine phosphatase activity
B1902584biological_processpositive regulation of response to water deprivation
C0004864molecular_functionprotein phosphatase inhibitor activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005773cellular_componentvacuole
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0009705cellular_componentplant-type vacuole membrane
C0009738biological_processabscisic acid-activated signaling pathway
C0010427molecular_functionabscisic acid binding
C0038023molecular_functionsignaling receptor activity
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0044389molecular_functionubiquitin-like protein ligase binding
C0062049cellular_componentprotein phosphatase inhibitor complex
C0080163biological_processregulation of protein serine/threonine phosphatase activity
C1902584biological_processpositive regulation of response to water deprivation
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PYV A 300
ChainResidue
ALYS59
AHOH218
AHIS60
APHE61
ALEU87
ASER92
AGLU94
ATYR120
AVAL163
AHOH216

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 192
ChainResidue
ALYS59
AHIS60
ALYS170
AHOH206
BGLY150
BASN151
BSER152

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 193
ChainResidue
ASER85
AGLY86
BSER88
BHOH202

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE P2M B 300
ChainResidue
BLYS59
BILE62
BLEU87
BSER92
BGLU94
BTYR120
BVAL163

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 192
ChainResidue
BHIS60

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PYV C 300
ChainResidue
CILE62
CVAL81
CLEU87
CSER92
CGLU94
CLEU117
CPHE159
CVAL163
CHOH219
CHOH222
CHOH223

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C 192
ChainResidue
CHIS60
CLYS170

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:19898494, ECO:0000269|PubMed:19933100
ChainResidueDetails
ALYS59
CALA89
CARG116
CGLU141
AALA89
AARG116
AGLU141
BLYS59
BALA89
BARG116
BGLU141
CLYS59

site_idSWS_FT_FI2
Number of Residues6
DetailsSITE: Involved in interactions with PP2Cs => ECO:0000269|PubMed:19407142
ChainResidueDetails
ASER88
ASER152
BSER88
BSER152
CSER88
CSER152

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphothreonine; by CARK1 => ECO:0000269|PubMed:29928509
ChainResidueDetails
ATHR78
BTHR78
CTHR78

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PDB entries from 2024-07-24

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