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5KA1

Protein Tyrosine Phosphatase 1B Delta helix 7 mutant in complex with TCS401, closed 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 Residues15
Detailsbinding site for residue OTA A 301
ChainResidue
ATYR46
AGLY220
AARG221
AGOL309
AHOH428
AHOH486
AHOH487
AASP48
ALYS120
AASP181
APHE182
ACYS215
ASER216
AALA217
AILE219

site_idAC2
Number of Residues4
Detailsbinding site for residue CL A 302
ChainResidue
AARG112
AVAL113
AHIS175
AHOH485

site_idAC3
Number of Residues3
Detailsbinding site for residue CL A 303
ChainResidue
AARG45
AHOH582
AHOH585

site_idAC4
Number of Residues6
Detailsbinding site for residue CL A 304
ChainResidue
ATYR20
AARG24
AARG254
AGLY259
AGLN262
AGOL309

site_idAC5
Number of Residues5
Detailsbinding site for residue CL A 305
ChainResidue
AARG238
ASER243
AVAL244
AASP245
AGOL311

site_idAC6
Number of Residues3
Detailsbinding site for residue TRS A 306
ChainResidue
AHIS54
AHOH483
AHOH576

site_idAC7
Number of Residues2
Detailsbinding site for residue DMS A 307
ChainResidue
AASP29
APHE30

site_idAC8
Number of Residues3
Detailsbinding site for residue DMS A 308
ChainResidue
APHE196
AARG199
AGLU200

site_idAC9
Number of Residues7
Detailsbinding site for residue GOL A 309
ChainResidue
AASP48
AMET258
AGLY259
AGLN262
AOTA301
ACL304
AHOH404

site_idAD1
Number of Residues4
Detailsbinding site for residue GOL A 310
ChainResidue
APRO89
AGLN123
AMET133
AHOH468

site_idAD2
Number of Residues8
Detailsbinding site for residue GOL A 311
ChainResidue
AGLU76
AARG238
ALYS248
AGLU252
ACL305
AHOH445
AHOH446
AHOH543

site_idAD3
Number of Residues5
Detailsbinding site for residue GOL A 312
ChainResidue
AGLN61
AGLU62
AASP63
AASN64
AASP65

site_idAD4
Number of Residues7
Detailsbinding site for residue GOL A 313
ChainResidue
ALYS103
APRO206
AGLU207
AHIS208
AGLY209
AHOH495
AHOH508

site_idAD5
Number of Residues5
Detailsbinding site for residue GOL A 314
ChainResidue
APRO31
ACYS32
AARG33
ALYS36
AHOH433

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 Residues1
DetailsACT_SITE: Phosphocysteine intermediate
ChainResidueDetails
ACYS215

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AASP181

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ACYS215
AGLN262

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|PubMed:2546149
ChainResidueDetails
AMET1

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR20

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKB/AKT1, CLK1 and CLK2 => ECO:0000269|PubMed:10480872, ECO:0000269|PubMed:11579209, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER50

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by EGFR => ECO:0000269|PubMed:9355745
ChainResidueDetails
ATYR66

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine; in reversibly inhibited form => ECO:0000269|PubMed:22169477
ChainResidueDetails
ACYS215

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CLK1 and CLK2 => ECO:0000269|PubMed:10480872
ChainResidueDetails
ASER242
ASER243

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form => ECO:0000269|PubMed:12802338, ECO:0000269|PubMed:12802339
ChainResidueDetails
ACYS215
ASER216

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

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PDB entries from 2024-07-24

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