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6KRX

Crystal Structure of AtPTP1 at 1.7 angstrom

Functional Information from GO Data
ChainGOidnamespacecontents
A0004721molecular_functionphosphoprotein phosphatase activity
A0004725molecular_functionprotein tyrosine phosphatase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006470biological_processprotein dephosphorylation
A0006952biological_processdefense response
A0016311biological_processdephosphorylation
A0019900molecular_functionkinase binding
A0031348biological_processnegative regulation of defense response
A0033550molecular_functionMAP kinase tyrosine phosphatase activity
A0035556biological_processintracellular signal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue IOD A 501
ChainResidue
AGLY308

site_idAC2
Number of Residues2
Detailsbinding site for residue IOD A 502
ChainResidue
AARG271
AHOH659

site_idAC3
Number of Residues13
Detailsbinding site for residue FLC A 503
ChainResidue
AALA267
AGLY268
AILE269
AGLY270
AARG271
AGLN311
AGLN315
ATYR93
ALYS174
AASP234
AHIS235
ACYS265
ASER266

Functional Information from PROSITE/UniProt
site_idPS00383
Number of Residues11
DetailsTYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsaGigRTG
ChainResidueDetails
AVAL263-GLY273

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Phosphocysteine intermediate
ChainResidueDetails
ACYS265

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AASP234

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ACYS265
AGLN311

226707

PDB entries from 2024-10-30

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