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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
DetailsACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMed:17139078
ChainResidueDetails
AGLY1909

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AGLU1875

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATYR1953
AGLY1909

219869

PDB entries from 2024-05-15

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