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5AES

Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphatase) in Complex with a PNP-derived Inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004721molecular_functionphosphoprotein phosphatase activity
A0004722molecular_functionprotein serine/threonine phosphatase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005911cellular_componentcell-cell junction
A0006338biological_processchromatin remodeling
A0006357biological_processregulation of transcription by RNA polymerase II
A0006470biological_processprotein dephosphorylation
A0007088biological_processregulation of mitotic nuclear division
A0015629cellular_componentactin cytoskeleton
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0017018molecular_functionmyosin phosphatase activity
A0030027cellular_componentlamellipodium
A0030496cellular_componentmidbody
A0030836biological_processpositive regulation of actin filament depolymerization
A0031072molecular_functionheat shock protein binding
A0031247biological_processactin rod assembly
A0031258cellular_componentlamellipodium membrane
A0032154cellular_componentcleavage furrow
A0032361biological_processpyridoxal phosphate catabolic process
A0032465biological_processregulation of cytokinesis
A0032587cellular_componentruffle membrane
A0033192molecular_functioncalmodulin-dependent protein phosphatase activity
A0033883molecular_functionpyridoxal phosphatase activity
A0042803molecular_functionprotein homodimerization activity
A0042995cellular_componentcell projection
A0046872molecular_functionmetal ion binding
A0070938cellular_componentcontractile ring
A0071318biological_processcellular response to ATP
A0098794cellular_componentpostsynapse
A0098978cellular_componentglutamatergic synapse
A0099159biological_processregulation of modification of postsynaptic structure
A0140791molecular_functionhistone H2AXS140 phosphatase activity
A0180004molecular_functionRNA polymerase II CTD heptapeptide repeat Y1 phosphatase activity
A0180005molecular_functionRNA polymerase II CTD heptapeptide repeat T4 phosphatase activity
A0180006molecular_functionRNA polymerase II CTD heptapeptide repeat S2 phosphatase activity
A0180007molecular_functionRNA polymerase II CTD heptapeptide repeat S5 phosphatase activity
A0180008molecular_functionRNA polymerase II CTD heptapeptide repeat S7 phosphatase activity
A1990439molecular_functionMAP kinase serine/threonine phosphatase activity
B0000287molecular_functionmagnesium ion binding
B0004721molecular_functionphosphoprotein phosphatase activity
B0004722molecular_functionprotein serine/threonine phosphatase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005886cellular_componentplasma membrane
B0005911cellular_componentcell-cell junction
B0006338biological_processchromatin remodeling
B0006357biological_processregulation of transcription by RNA polymerase II
B0006470biological_processprotein dephosphorylation
B0007088biological_processregulation of mitotic nuclear division
B0015629cellular_componentactin cytoskeleton
B0016311biological_processdephosphorylation
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0017018molecular_functionmyosin phosphatase activity
B0030027cellular_componentlamellipodium
B0030496cellular_componentmidbody
B0030836biological_processpositive regulation of actin filament depolymerization
B0031072molecular_functionheat shock protein binding
B0031247biological_processactin rod assembly
B0031258cellular_componentlamellipodium membrane
B0032154cellular_componentcleavage furrow
B0032361biological_processpyridoxal phosphate catabolic process
B0032465biological_processregulation of cytokinesis
B0032587cellular_componentruffle membrane
B0033192molecular_functioncalmodulin-dependent protein phosphatase activity
B0033883molecular_functionpyridoxal phosphatase activity
B0042803molecular_functionprotein homodimerization activity
B0042995cellular_componentcell projection
B0046872molecular_functionmetal ion binding
B0070938cellular_componentcontractile ring
B0071318biological_processcellular response to ATP
B0098794cellular_componentpostsynapse
B0098978cellular_componentglutamatergic synapse
B0099159biological_processregulation of modification of postsynaptic structure
B0140791molecular_functionhistone H2AXS140 phosphatase activity
B0180004molecular_functionRNA polymerase II CTD heptapeptide repeat Y1 phosphatase activity
B0180005molecular_functionRNA polymerase II CTD heptapeptide repeat T4 phosphatase activity
B0180006molecular_functionRNA polymerase II CTD heptapeptide repeat S2 phosphatase activity
B0180007molecular_functionRNA polymerase II CTD heptapeptide repeat S5 phosphatase activity
B0180008molecular_functionRNA polymerase II CTD heptapeptide repeat S7 phosphatase activity
B1990439molecular_functionMAP kinase serine/threonine phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 305
ChainResidue
AASP25
AASP27
AASP234
A5B0306
AHOH2002
AHOH2003

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 5B0 A 306
ChainResidue
ASER58
AASN59
AASN60
ATYR146
AHIS178
ALYS209
AMG305
AHOH2002
AHOH2003
AHOH2018
AASP25
ACYS26
AASP27

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 305
ChainResidue
BASP25
BASP27
BASP234
B5B0306
BHOH2001
BHOH2002

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 5B0 B 306
ChainResidue
BASP25
BCYS26
BASP27
BSER58
BASN59
BASN60
BARG62
BTYR146
BHIS178
BLYS209
BMG305
BGOL1292
BHOH2001
BHOH2002
BHOH2003

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1292
ChainResidue
BASP27
BTRP31
BASN60
BARG62
BARG63
B5B0306

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:24338687, ECO:0000305|PubMed:25783190, ECO:0007744|PDB:4BX2, ECO:0007744|PDB:5AES
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:24338687, ECO:0000305|PubMed:25783190, ECO:0007744|PDB:4BX2, ECO:0007744|PDB:5AES
ChainResidueDetails
AASP27
BASP27

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:24338473, ECO:0000269|PubMed:24338687, ECO:0000269|PubMed:25783190, ECO:0007744|PDB:4BKM, ECO:0007744|PDB:4BX0, ECO:0007744|PDB:4BX2, ECO:0007744|PDB:4BX3, ECO:0007744|PDB:5AES
ChainResidueDetails
AASP25
AASP27
AASP234
BASP25
BASP27
BASP234

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:24338687, ECO:0000269|PubMed:25783190, ECO:0007744|PDB:4BX2, ECO:0007744|PDB:5AES
ChainResidueDetails
ASER58
ALYS209
BSER58
BLYS209

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:25783190, ECO:0007744|PDB:5AES
ChainResidueDetails
AHIS178
BHIS178

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PDB entries from 2024-11-13

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