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2CM3

Structure of Protein Tyrosine Phosphatase 1B (C2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004725molecular_functionprotein tyrosine phosphatase activity
A0006470biological_processprotein dephosphorylation
A0016311biological_processdephosphorylation
B0004725molecular_functionprotein tyrosine phosphatase activity
B0006470biological_processprotein dephosphorylation
B0016311biological_processdephosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CA A1282
ChainResidue
AHIS54
AHOH2070
AHOH2071
AHOH2072
BLYS128
BHOH2149
BHOH2152
BHOH2154
BHOH2155

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B1282
ChainResidue
AHOH2148
AHOH2152
BHIS54
BHOH2077
BHOH2079
BHOH2080

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 Residues2
DetailsACT_SITE: Phosphocysteine intermediate
ChainResidueDetails
ACYS215
BCYS215

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AASP181
BASP181

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ACYS215
AGLN262
BCYS215
BGLN262

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|PubMed:2546149
ChainResidueDetails
AMET-5
BMET-5

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR20
BTYR20

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKB/AKT1, CLK1 and CLK2 => ECO:0000269|PubMed:10480872, ECO:0000269|PubMed:11579209, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER50
BSER50

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by EGFR => ECO:0000269|PubMed:9355745
ChainResidueDetails
ATYR66
BTYR66

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine; in reversibly inhibited form => ECO:0000269|PubMed:22169477
ChainResidueDetails
ACYS215
BCYS215

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphoserine; by CLK1 and CLK2 => ECO:0000269|PubMed:10480872
ChainResidueDetails
ASER242
ASER243
BSER242
BSER243

site_idSWS_FT_FI10
Number of Residues4
DetailsCROSSLNK: N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form => ECO:0000269|PubMed:12802338, ECO:0000269|PubMed:12802339
ChainResidueDetails
ACYS215
ASER216
BCYS215
BSER216

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d5r
ChainResidueDetails
AARG221
AASP181
ACYS215

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d5r
ChainResidueDetails
BARG221
BASP181
BCYS215

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d5r
ChainResidueDetails
AARG221
AASP181
ACYS215
ASER222

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d5r
ChainResidueDetails
BARG221
BASP181
BCYS215
BSER222

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

site_idMCSA2
Number of Residues5
DetailsM-CSA 469
ChainResidueDetails
BASP181proton shuttle (general acid/base)
BCYS215covalent catalysis
BARG221activator, electrostatic stabiliser
BSER222activator, electrostatic stabiliser
BGLN262steric role

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PDB entries from 2024-06-26

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