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2H03

Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors

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 Residues5
DetailsBINDING SITE FOR RESIDUE CL A 302
ChainResidue
AGLY1765
AASN1766
AASN1767
APHE1768
AARG1970

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG A 303
ChainResidue
AHOH74
AHOH74
AHOH76
AHOH76
AHOH56
AHOH56
AHOH57
AHOH57

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 304
ChainResidue
AHOH59
AHOH203
AHOH213
AHOH227
AASP1827
AGLU1851

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 305
ChainResidue
ATYR1762
APRO1764
AARG1769
AARG1770

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 3UN A 401
ChainResidue
AHOH22
AASP1720
ALEU1723
ATYR1733
AASN1734
AASN1735
ALYS1811
AASP1870
AHIS1871
ACYS1904
ASER1905
AALA1906
AGLY1907
AVAL1908
AGLY1909
AARG1910
AHIS1945
AGLN1948

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
DetailsActive site: {"description":"Phosphocysteine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10044","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17139078","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1ytw
ChainResidueDetails
AARG1910
AGLU1806
ACYS1904
AASP1870
ATHR1911
AHIS1903

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ytw
ChainResidueDetails
AARG1910
ACYS1904
AASP1870
ATHR1911

239803

PDB entries from 2025-08-06

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