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1FJM

Protein serine/threonine phosphatase-1 (alpha isoform, type 1) complexed with microcystin-LR toxin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000164cellular_componentprotein phosphatase type 1 complex
A0004721molecular_functionphosphoprotein phosphatase activity
A0004722molecular_functionprotein serine/threonine phosphatase activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005977biological_processglycogen metabolic process
A0006446biological_processregulation of translational initiation
A0006470biological_processprotein dephosphorylation
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0017018molecular_functionmyosin phosphatase activity
A0032922biological_processcircadian regulation of gene expression
A0042752biological_processregulation of circadian rhythm
A0043153biological_processentrainment of circadian clock by photoperiod
A0043558biological_processregulation of translational initiation in response to stress
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal ion binding
A0048511biological_processrhythmic process
A0051301biological_processcell division
A0072357cellular_componentPTW/PP1 phosphatase complex
A0072542molecular_functionprotein phosphatase activator activity
A0090263biological_processpositive regulation of canonical Wnt signaling pathway
A1901567molecular_functionfatty acid derivative binding
B0000164cellular_componentprotein phosphatase type 1 complex
B0004721molecular_functionphosphoprotein phosphatase activity
B0004722molecular_functionprotein serine/threonine phosphatase activity
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0005977biological_processglycogen metabolic process
B0006446biological_processregulation of translational initiation
B0006470biological_processprotein dephosphorylation
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0017018molecular_functionmyosin phosphatase activity
B0032922biological_processcircadian regulation of gene expression
B0042752biological_processregulation of circadian rhythm
B0043153biological_processentrainment of circadian clock by photoperiod
B0043558biological_processregulation of translational initiation in response to stress
B0046872molecular_functionmetal ion binding
B0046914molecular_functiontransition metal ion binding
B0048511biological_processrhythmic process
B0051301biological_processcell division
B0072357cellular_componentPTW/PP1 phosphatase complex
B0072542molecular_functionprotein phosphatase activator activity
B0090263biological_processpositive regulation of canonical Wnt signaling pathway
B1901567molecular_functionfatty acid derivative binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 400
ChainResidue
AASP92
AASN124
AHIS173
AHIS248
AMN401
AHOH402

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 401
ChainResidue
AMN400
AHOH402
MHOH8
AASP64
AHIS66
AASP92

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME A 399
ChainResidue
APHE257
AARG261
ACYS291

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 400
ChainResidue
BASP92
BASN124
BHIS173
BHIS248
BMN401
BHOH402

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 401
ChainResidue
BASP64
BHIS66
BASP92
BMN400
BHOH402
NHOH128

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME B 399
ChainResidue
BILE169
BLEU289
BMET290
BCYS291
BHOH536

Functional Information from PROSITE/UniProt
site_idPS00125
Number of Residues6
DetailsSER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE
ChainResidueDetails
ALEU121-GLU126

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AHIS125
BHIS125

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AASP64
BASN124
BHIS173
BHIS248
AHIS66
AASP92
AASN124
AHIS173
AHIS248
BASP64
BHIS66
BASP92

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62136
ChainResidueDetails
ASER2
ASER22
ASER325
BSER2
BSER22
BSER325

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P62137
ChainResidueDetails
ALYS305
BLYS305

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62137
ChainResidueDetails
ATYR306
BTYR306

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62136
ChainResidueDetails
ATHR320
BTHR320

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aui
ChainResidueDetails
AASP95
AHIS125

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aui
ChainResidueDetails
BASP95
BHIS125

225946

PDB entries from 2024-10-09

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