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1Q6P

THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE 1B IN COMPLEX WITH COMPOUND 6

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 Residues3
DetailsBINDING SITE FOR RESIDUE CL A 2001
ChainResidue
AARG524
AARG754
AGLN762

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 213 A 801
ChainResidue
AALA717
AGLY718
AILE719
AGLY720
AARG721
AMET758
AGLY759
AGLN762
AHOH3035
BALA1018
BGLN1021
BARG1024
ATYR546
AARG547
AASP548
APHE682
ACYS715
ASER716

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE 213 B 1301
ChainResidue
AALA518
AASP522
AHIS525
AGLU526
BTYR1020
BARG1024
BTYR1046
BARG1047
BASP1048
BLEU1119
BPHE1182
BCYS1215
BSER1216
BALA1217
BGLY1218
BILE1219
BGLY1220
BARG1221
BARG1254
BMET1258
BGLN1262
BHOH3081
BHOH3140
BHOH3204

Functional Information from PROSITE/UniProt
site_idPS00383
Number of Residues11
DetailsTYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsaGigRSG
ChainResidueDetails
AVAL713-GLY723

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Phosphocysteine intermediate
ChainResidueDetails
ACYS715
BCYS1215

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AASP681
BASP1181

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ACYS715
AGLN762
BCYS1215
BGLN1262

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|PubMed:2546149
ChainResidueDetails
AMET501
BMET1001

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR520
BTYR1020

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
ASER550
BSER1050

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by EGFR => ECO:0000269|PubMed:9355745
ChainResidueDetails
ATYR566
BTYR1066

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine; in reversibly inhibited form => ECO:0000269|PubMed:22169477
ChainResidueDetails
ACYS715
BCYS1215

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphoserine; by CLK1 and CLK2 => ECO:0000269|PubMed:10480872
ChainResidueDetails
ASER742
ASER743
BSER1242
BSER1243

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
ACYS715
ASER716
BCYS1215
BSER1216

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d5r
ChainResidueDetails
AARG721
ACYS715
AASP681

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d5r
ChainResidueDetails
BASP1181
BARG1221
BCYS1215

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d5r
ChainResidueDetails
AARG721
ASER722
ACYS715
AASP681

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d5r
ChainResidueDetails
BASP1181
BSER1222
BARG1221
BCYS1215

site_idMCSA1
Number of Residues5
DetailsM-CSA 469
ChainResidueDetails
AASP681proton shuttle (general acid/base)
ACYS715covalent catalysis
AARG721activator, electrostatic stabiliser
ASER722activator, electrostatic stabiliser
AGLN762steric role

site_idMCSA2
Number of Residues5
DetailsM-CSA 469
ChainResidueDetails
BASP1181proton shuttle (general acid/base)
BCYS1215covalent catalysis
BARG1221activator, electrostatic stabiliser
BSER1222activator, electrostatic stabiliser
BGLN1262steric role

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PDB entries from 2024-07-24

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