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3HVQ

Crystal structure of a complex between Protein Phosphatase 1 alpha (PP1) and the PP1 binding and PDZ domains of Neurabin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000164cellular_componentprotein phosphatase type 1 complex
A0000781cellular_componentchromosome, telomeric region
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
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005912cellular_componentadherens junction
A0005977biological_processglycogen metabolic process
A0005979biological_processregulation of glycogen biosynthetic process
A0005981biological_processregulation of glycogen catabolic process
A0006470biological_processprotein dephosphorylation
A0008157molecular_functionprotein phosphatase 1 binding
A0010288biological_processresponse to lead ion
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0017018molecular_functionmyosin phosphatase activity
A0030324biological_processlung development
A0032922biological_processcircadian regulation of gene expression
A0042587cellular_componentglycogen granule
A0042752biological_processregulation of circadian rhythm
A0043021molecular_functionribonucleoprotein complex binding
A0043025cellular_componentneuronal cell body
A0043153biological_processentrainment of circadian clock by photoperiod
A0043197cellular_componentdendritic spine
A0043204cellular_componentperikaryon
A0043247biological_processtelomere maintenance in response to DNA damage
A0043558biological_processregulation of translational initiation in response to stress
A0044877molecular_functionprotein-containing complex binding
A0045725biological_processpositive regulation of glycogen biosynthetic process
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal ion binding
A0048754biological_processbranching morphogenesis of an epithelial tube
A0051301biological_processcell division
A0060828biological_processregulation of canonical Wnt signaling pathway
A0070062cellular_componentextracellular exosome
A0072357cellular_componentPTW/PP1 phosphatase complex
A0098609biological_processcell-cell adhesion
A0098641molecular_functioncadherin binding involved in cell-cell adhesion
A0098793cellular_componentpresynapse
A0098794cellular_componentpostsynapse
A0098978cellular_componentglutamatergic synapse
A2001241biological_processpositive regulation of extrinsic apoptotic signaling pathway in absence of ligand
B0000164cellular_componentprotein phosphatase type 1 complex
B0000781cellular_componentchromosome, telomeric region
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
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005912cellular_componentadherens junction
B0005977biological_processglycogen metabolic process
B0005979biological_processregulation of glycogen biosynthetic process
B0005981biological_processregulation of glycogen catabolic process
B0006470biological_processprotein dephosphorylation
B0008157molecular_functionprotein phosphatase 1 binding
B0010288biological_processresponse to lead ion
B0016311biological_processdephosphorylation
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0017018molecular_functionmyosin phosphatase activity
B0030324biological_processlung development
B0032922biological_processcircadian regulation of gene expression
B0042587cellular_componentglycogen granule
B0042752biological_processregulation of circadian rhythm
B0043021molecular_functionribonucleoprotein complex binding
B0043025cellular_componentneuronal cell body
B0043153biological_processentrainment of circadian clock by photoperiod
B0043197cellular_componentdendritic spine
B0043204cellular_componentperikaryon
B0043247biological_processtelomere maintenance in response to DNA damage
B0043558biological_processregulation of translational initiation in response to stress
B0044877molecular_functionprotein-containing complex binding
B0045725biological_processpositive regulation of glycogen biosynthetic process
B0046872molecular_functionmetal ion binding
B0046914molecular_functiontransition metal ion binding
B0048754biological_processbranching morphogenesis of an epithelial tube
B0051301biological_processcell division
B0060828biological_processregulation of canonical Wnt signaling pathway
B0070062cellular_componentextracellular exosome
B0072357cellular_componentPTW/PP1 phosphatase complex
B0098609biological_processcell-cell adhesion
B0098641molecular_functioncadherin binding involved in cell-cell adhesion
B0098793cellular_componentpresynapse
B0098794cellular_componentpostsynapse
B0098978cellular_componentglutamatergic synapse
B2001241biological_processpositive regulation of extrinsic apoptotic signaling pathway in absence of ligand
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN A 1
ChainResidue
AASP64
AHIS66
AASP92
AMN331
APO4332
AHOH333
AHOH335

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN A 331
ChainResidue
AASN124
AHIS173
AHIS248
APO4332
AHOH335
AMN1
AASP92

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PO4 A 332
ChainResidue
AMN1
AHIS66
AASP92
AARG96
AASN124
AHIS125
AARG221
AHIS248
AMN331
AHOH333
AHOH335
AHOH507
AHOH510

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN B 331
ChainResidue
BASP64
BHIS66
BASP92
BMN332
BPO4333
BHOH337
BHOH338

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN B 332
ChainResidue
BASP92
BASN124
BHIS173
BHIS248
BMN331
BPO4333
BHOH338

site_idAC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PO4 B 333
ChainResidue
BHIS66
BASP92
BARG96
BASN124
BHIS125
BARG221
BHIS248
BTYR272
BMN331
BMN332
BHOH337
BHOH338
BHOH513
BHOH515
BHOH516

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1
ChainResidue
ALYS26
BGLY14
BARG15
BGLU18
BHOH336
BHOH341

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 334
ChainResidue
BLYS260
BHOH432

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 335
ChainResidue
BCYS127
BSER129
BILE130
BVAL195
BASP197
BTRP206
BHOH422

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 Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP64
AHIS66
BASP64
BHIS66

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AASP92
AASN124
AHIS173
AHIS248
BASP92
BASN124
BHIS173
BHIS248

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER22
ASER325
BSER22
BSER325

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P62137
ChainResidueDetails
ALYS305
BLYS305

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62137
ChainResidueDetails
ATYR306
BTYR306

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:16732323, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR320
BTHR320

226707

PDB entries from 2024-10-30

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