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4H1O

Crystal structure of the tyrosine phosphatase SHP-2 with D61G mutation

Functional Information from GO Data
ChainGOidnamespacecontents
A0001784molecular_functionphosphotyrosine residue binding
A0004721molecular_functionphosphoprotein phosphatase activity
A0004725molecular_functionprotein tyrosine phosphatase activity
A0004726molecular_functionnon-membrane spanning protein tyrosine phosphatase activity
A0005158molecular_functioninsulin receptor binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0006470biological_processprotein dephosphorylation
A0007173biological_processepidermal growth factor receptor signaling pathway
A0007420biological_processbrain development
A0007507biological_processheart development
A0008543biological_processfibroblast growth factor receptor signaling pathway
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
A0019221biological_processcytokine-mediated signaling pathway
A0019901molecular_functionprotein kinase binding
A0030159molecular_functionsignaling receptor complex adaptor activity
A0030971molecular_functionreceptor tyrosine kinase binding
A0031295biological_processT cell costimulation
A0031666biological_processpositive regulation of lipopolysaccharide-mediated signaling pathway
A0032331biological_processnegative regulation of chondrocyte differentiation
A0032480biological_processnegative regulation of type I interferon production
A0032728biological_processpositive regulation of interferon-beta production
A0032760biological_processpositive regulation of tumor necrosis factor production
A0032991cellular_componentprotein-containing complex
A0033629biological_processnegative regulation of cell adhesion mediated by integrin
A0035335biological_processpeptidyl-tyrosine dephosphorylation
A0036302biological_processatrioventricular canal development
A0038127biological_processERBB signaling pathway
A0042130biological_processnegative regulation of T cell proliferation
A0042311biological_processvasodilation
A0043254biological_processregulation of protein-containing complex assembly
A0045296molecular_functioncadherin binding
A0045778biological_processpositive regulation of ossification
A0046326biological_processpositive regulation of D-glucose import
A0046628biological_processpositive regulation of insulin receptor signaling pathway
A0048013biological_processephrin receptor signaling pathway
A0048806biological_processgenitalia development
A0048839biological_processinner ear development
A0050839molecular_functioncell adhesion molecule binding
A0050860biological_processnegative regulation of T cell receptor signaling pathway
A0050868biological_processnegative regulation of T cell activation
A0051428molecular_functionpeptide hormone receptor binding
A0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A0060090molecular_functionmolecular adaptor activity
A0060325biological_processface morphogenesis
A0060338biological_processregulation of type I interferon-mediated signaling pathway
A0070374biological_processpositive regulation of ERK1 and ERK2 cascade
A0071260biological_processcellular response to mechanical stimulus
A0071364biological_processcellular response to epidermal growth factor stimulus
A1902533biological_processpositive regulation of intracellular signal transduction
A1902564biological_processnegative regulation of neutrophil activation
A1990782molecular_functionprotein tyrosine kinase binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 601
ChainResidue
ASER3
ATRP6
ACYS259

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 602
ChainResidue
AGLN335
ALYS369
AGLU532
AHOH734

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 603
ChainResidue
AHIS520
AMET516
AGLN519

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 604
ChainResidue
ALYS131
ASER165

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 605
ChainResidue
AGLY60
ATRP423
AGLY427
AVAL428
AARG465
AGLN510
AHOH782

Functional Information from PROSITE/UniProt
site_idPS00383
Number of Residues11
DetailsTYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsaGigRTG
ChainResidueDetails
AVAL457-GLY467

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Phosphocysteine intermediate"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N-acetylthreonine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P35235","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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