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5KAA

Protein Tyrosine Phosphatase 1B Delta helix 7, P185G mutant, open state

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 Residues2
Detailsbinding site for residue CL A 301
ChainResidue
APRO38
ALYS39

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 302
ChainResidue
AARG24
AARG254

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 303
ChainResidue
AVAL113
AHIS175

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 304
ChainResidue
ASER151
AASP181

site_idAC5
Number of Residues3
Detailsbinding site for residue CL A 305
ChainResidue
AARG199
ALYS239
AARG79

site_idAC6
Number of Residues4
Detailsbinding site for residue CL A 306
ChainResidue
ALYS120
ACYS215
ASER216
AARG221

site_idAC7
Number of Residues3
Detailsbinding site for residue CL A 307
ChainResidue
AARG238
ASER243
AASP245

site_idAC8
Number of Residues5
Detailsbinding site for residue CL A 308
ChainResidue
AMET74
AGLU76
AALA77
AHOH464
AHOH558

site_idAC9
Number of Residues6
Detailsbinding site for residue TRS A 309
ChainResidue
AHIS54
ALYS128
AGLU129
AGLU130
AHOH411
AHOH534

site_idAD1
Number of Residues6
Detailsbinding site for residue GOL A 310
ChainResidue
APRO89
ACYS92
AMET133
APHE135
AHOH413
AHOH433

site_idAD2
Number of Residues5
Detailsbinding site for residue GOL A 311
ChainResidue
ATYR46
AVAL49
AGLN262
AHOH447
AHOH560

Functional Information from PROSITE/UniProt
site_idPS00383
Number of Residues11
DetailsTYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsaGigRSG
ChainResidueDetails
AVAL213-GLY223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues274
DetailsDomain: {"description":"Tyrosine-protein phosphatase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Phosphocysteine intermediate"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"2546149","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKB/AKT1, CLK1 and CLK2","evidences":[{"source":"PubMed","id":"10480872","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11579209","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by EGFR","evidences":[{"source":"PubMed","id":"9355745","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"S-nitrosocysteine; in reversibly inhibited form","evidences":[{"source":"PubMed","id":"22169477","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by CLK1 and CLK2","evidences":[{"source":"PubMed","id":"10480872","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsCross-link: {"description":"N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form","evidences":[{"source":"PubMed","id":"12802338","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12802339","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 469
ChainResidueDetails
AASP181proton shuttle (general acid/base)
ACYS215covalent catalysis
AARG221activator, electrostatic stabiliser
ASER222activator, electrostatic stabiliser
AGLN262steric role

246031

PDB entries from 2025-12-10

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