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2NT2

Crystal Structure of Slingshot phosphatase 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0003779molecular_functionactin binding
A0006470biological_processprotein dephosphorylation
A0016311biological_processdephosphorylation
A0016791molecular_functionphosphatase activity
A0030837biological_processnegative regulation of actin filament polymerization
B0003779molecular_functionactin binding
B0006470biological_processprotein dephosphorylation
B0016311biological_processdephosphorylation
B0016791molecular_functionphosphatase activity
B0030837biological_processnegative regulation of actin filament polymerization
C0003779molecular_functionactin binding
C0006470biological_processprotein dephosphorylation
C0016311biological_processdephosphorylation
C0016791molecular_functionphosphatase activity
C0030837biological_processnegative regulation of actin filament polymerization
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 101
ChainResidue
AASP361
ASER392
ALYS393
AMET394
AGLY395
AVAL396
ASER397
AARG398

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 101
ChainResidue
BSER392
BLYS393
BMET394
BGLY395
BVAL396
BSER397
BARG398
BASP361

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 C 101
ChainResidue
CHOH66
CASP361
CSER392
CLYS393
CMET394
CGLY395
CVAL396
CSER397
CARG398

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues423
DetailsDomain: {"description":"Tyrosine-protein phosphatase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Phosphocysteine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17427953","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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