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2CFR

crystal structure of human pyridoxal 5'-phosphate phosphatase

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
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
A0033883molecular_functionpyridoxal phosphatase activity
A0042803molecular_functionprotein homodimerization activity
A0042995cellular_componentcell projection
A0046872molecular_functionmetal ion binding
A0070938cellular_componentcontractile ring
A0071318biological_processcellular response to ATP
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A1297
ChainResidue
AASP25
AASP27
AASP238

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:15580268, ECO:0000269|PubMed:18058037, ECO:0007744|PDB:2P27
ChainResidueDetails
AASP25

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:15580268, ECO:0000305|PubMed:18058037, ECO:0007744|PDB:2P27
ChainResidueDetails
AASP27

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:18058037, ECO:0007744|PDB:2P27
ChainResidueDetails
AASP25
ASER58
AHIS182
ALYS213
AASP238
AASP27

220472

PDB entries from 2024-05-29

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