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1Q6S

THE STRUCTURE OF PHOSPHOTYROSINE PHOSPHATASE 1B IN COMPLEX WITH COMPOUND 9

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 Residues2
DetailsBINDING SITE FOR RESIDUE CL A 2011
ChainResidue
AARG545
ALEU619

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 2012
ChainResidue
BARG1045
BALA1122

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 2013
ChainResidue
AHOH3307
BARG1047
B2141301

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 4000
ChainResidue
AHOH4003
AHOH4004
AHOH4005
AHOH4006
AHOH4001
AHOH4002

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG B 5000
ChainResidue
BHIS1054
BHOH3185
BHOH5001
BHOH5002
BHOH5003
BHOH5004
BHOH5005
BHOH5006

site_idAC6
Number of Residues27
DetailsBINDING SITE FOR RESIDUE 214 A 801
ChainResidue
AARG524
ASER528
AASP529
ATYR546
AARG547
AASP548
AASP681
APHE682
ACYS715
ASER716
AALA717
AGLY718
AILE719
AGLY720
AARG721
AARG754
AMET758
AGLN762
AHOH3005
AHOH3027
AHOH3031
AHOH3110
AHOH3194
AHOH3265
BALA1018
BGLN1021
BASP1022

site_idAC7
Number of Residues30
DetailsBINDING SITE FOR RESIDUE 214 B 1301
ChainResidue
AALA518
AASP522
AHIS525
AGLU526
BARG1024
BSER1028
BASP1029
BTYR1046
BARG1047
BASP1048
BLEU1119
BPHE1182
BCYS1215
BSER1216
BALA1217
BGLY1218
BILE1219
BGLY1220
BARG1221
BARG1254
BMET1258
BGLY1259
BGLN1262
BCL2013
BHOH3033
BHOH3036
BHOH3058
BHOH3064
BHOH3073
BHOH3120

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 6000
ChainResidue
AARG524
AHOH3097
AHOH3103
BALA1017
BTYR1020
BARG1024

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

222415

PDB entries from 2024-07-10

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