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2I4H

Structural studies of protein tyrosine phosphatase beta catalytic domain co-crystallized with a sulfamic acid inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004725molecular_functionprotein tyrosine phosphatase activity
A0006470biological_processprotein dephosphorylation
A0016311biological_processdephosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG A 202
ChainResidue
AHOH58
AHOH58
AHOH59
AHOH59
AHOH60
AHOH60
AHOH61
AHOH61

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 203
ChainResidue
AASN1767
APHE1768
AARG1970
AGLY1765

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE UA1 A 401
ChainResidue
AHOH125
AARG1715
AASN1716
ASER1718
AASP1720
AARG1732
ATYR1733
AASN1734
AASN1735
ALYS1807
AGLY1808
AASP1870
AHIS1871
ACYS1904
ASER1905
AALA1906
AGLY1907
AVAL1908
AGLY1909
AARG1910

Functional Information from PROSITE/UniProt
site_idPS00383
Number of Residues11
DetailsTYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsaGvgRTG
ChainResidueDetails
AVAL1902-GLY1912

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMed:17139078
ChainResidueDetails
ACYS1904

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AASP1870

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLN1948
ACYS1904

221051

PDB entries from 2024-06-12

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