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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 Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:20729862, ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV, ECO:0007744|PDB:3UJK, ECO:0007744|PDB:3UJL
ChainResidueDetails
BASP165
BASP337
BASP402
AGLU147

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20729862, ECO:0000269|PubMed:22116026, ECO:0007744|PDB:3NMV, ECO:0007744|PDB:3UJL
ChainResidueDetails
BASP251
BSER252

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Lock => ECO:0000250|UniProtKB:Q9CAJ0
ChainResidueDetails
BTRP290

218853

数据于2024-04-24公开中

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