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4J51

Cyrstal structure of protein tyrosine phosphatase Lyp catalytic domain complex with small molecular inhibitor L75N04

Functional Information from GO Data
ChainGOidnamespacecontents
A0004725molecular_functionprotein tyrosine phosphatase activity
A0004726molecular_functionnon-membrane spanning protein tyrosine phosphatase activity
A0006470biological_processprotein dephosphorylation
A0016311biological_processdephosphorylation
B0004725molecular_functionprotein tyrosine phosphatase activity
B0004726molecular_functionnon-membrane spanning protein tyrosine phosphatase activity
B0006470biological_processprotein dephosphorylation
B0016311biological_processdephosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE N75 A 401
ChainResidue
ATYR60
AGLN274
AGLN278
ALYS61
AASP62
ACYS227
ASER228
AALA229
ACYS231
AGLY232
AARG233

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE N75 B 401
ChainResidue
BTYR60
BLYS61
BASP62
BCYS227
BSER228
BALA229
BCYS231
BGLY232
BARG233
BGLN274
BTHR275
BGLN278
BHOH519

Functional Information from PROSITE/UniProt
site_idPS00383
Number of Residues11
DetailsTYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. IHCsaGcgRTG
ChainResidueDetails
AILE225-GLY235

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000255|PROSITE-ProRule:PRU10044
ChainResidueDetails
ACYS227
BCYS227

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|Ref.20
ChainResidueDetails
ACYS227
AGLN274
BCYS227
BGLN274

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKC/PRKCD => ECO:0000269|PubMed:18056643
ChainResidueDetails
ASER35
BSER35

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PDB entries from 2024-07-10

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