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5QEV

PanDDA analysis group deposition -- Crystal structure of PTP1B in complex with compound_XST00000603b

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 Residues4
Detailsbinding site for residue JKV A 401
ChainResidue
AASP29
APHE30
APRO31
AGLU170

site_idAC2
Number of Residues5
Detailsbinding site for residue TRS A 402
ChainResidue
AHIS54
ALYS128
AGLU129
AGLU130
AHOH584

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

226707

PDB entries from 2024-10-30

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