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2VX3

Crystal structure of the human dual specificity tyrosine- phosphorylation-regulated kinase 1A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004712molecular_functionprotein serine/threonine/tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0046777biological_processprotein autophosphorylation
B0004672molecular_functionprotein kinase activity
B0004712molecular_functionprotein serine/threonine/tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0046777biological_processprotein autophosphorylation
C0004672molecular_functionprotein kinase activity
C0004712molecular_functionprotein serine/threonine/tyrosine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
C0046777biological_processprotein autophosphorylation
D0004672molecular_functionprotein kinase activity
D0004712molecular_functionprotein serine/threonine/tyrosine kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
D0046777biological_processprotein autophosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE D15 A 600
ChainResidue
AGLY166
ALEU241
ASER242
AASN292
ALEU294
AASP307
ACL620
AP6G700
ASO41483
AHOH2035
ALYS167
AGLY168
AGLY171
AGLN172
AVAL173
AALA186
AGLU239
AMET240

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 620
ChainResidue
ALYS188
AASP307
AD15600

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE P6G A 700
ChainResidue
AASP162
ALYS175
AD15600

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE P6G A 701
ChainResidue
AGLN201
CGLN201

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE P6G A 702
ChainResidue
ATYR319

site_idAC6
Number of Residues18
DetailsBINDING SITE FOR RESIDUE D15 B 600
ChainResidue
BILE165
BGLY166
BGLY168
BGLY171
BGLN172
BVAL173
BALA186
BLYS188
BGLU239
BLEU241
BSER242
BASN292
BLEU294
BASP307
BCL620
BP6G700
BSO41482
DARG179

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 620
ChainResidue
BLYS188
BASP307
BD15600

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE P6G B 700
ChainResidue
BASP162
BLYS175
BMET240
BD15600

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE P6G B 701
ChainResidue
BGLN201
BHIS227
DGLN201
DLEU234

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE P6G B 702
ChainResidue
BASP247
BASN251
DGLU160

site_idBC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE D15 C 600
ChainResidue
CILE165
CGLY166
CLYS167
CGLY168
CGLY171
CVAL173
CALA186
CLYS188
CGLU239
CMET240
CLEU241
CSER242
CASN292
CLEU294
CASP307
CCL620
CSO41482

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL C 620
ChainResidue
CLYS188
CASP307
CD15600

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE P6G C 700
ChainResidue
CASP162
CLYS175
CTRP184

site_idBC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE D15 D 600
ChainResidue
DSO41482
DILE165
DGLY166
DLYS167
DGLY168
DGLY171
DGLN172
DVAL173
DALA186
DGLU239
DMET240
DLEU241
DSER242
DTYR243
DASN292
DLEU294
DASP307
DCL620

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL D 620
ChainResidue
DLYS188
DASP307
DD15600

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE P6G D 700
ChainResidue
DASP162
DLYS175
DTRP184

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 1482
ChainResidue
CGLY168
CSER169
CLYS289
CD15600
CHOH2026

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1483
ChainResidue
AGLY168
ASER169
ALYS289
AASP307
AASP410
AD15600

site_idCC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 1482
ChainResidue
CASP410
DGLY168
DSER169
DLYS289
DD15600

site_idCC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1482
ChainResidue
BSER169
BLYS289
BD15600

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1483
ChainResidue
BASN365
BGLU366
BLYS393
DARG300

site_idCC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C 1483
ChainResidue
CLYS225
CARG226

site_idCC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 1484
ChainResidue
CLYS264
CARG300
CSER301

site_idCC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1484
ChainResidue
BLYS264
BARG300
BSER301

site_idCC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 1485
ChainResidue
BHIS424
BLYS453

site_idCC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL D 1484
ChainResidue
BARG325

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSFGQVVkAydrveqew..........VAIK
ChainResidueDetails
AILE165-LYS188

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHcDLKpeNILL
ChainResidueDetails
AILE283-LEU295

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:23665168
ChainResidueDetails
AASP287
BASP287
CASP287
DASP287

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AILE165
DILE165
DLYS188
DPHE238
ALYS188
APHE238
BILE165
BLYS188
BPHE238
CILE165
CLYS188
CPHE238

site_idSWS_FT_FI3
Number of Residues24
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:23665168
ChainResidueDetails
ATYR140
BTYR319
BPTR321
BTYR449
CTYR140
CTYR159
CTYR177
CTYR319
CPTR321
CTYR449
DTYR140
ATYR159
DTYR159
DTYR177
DTYR319
DPTR321
DTYR449
ATYR177
ATYR319
APTR321
ATYR449
BTYR140
BTYR159
BTYR177

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR145
BTYR145
CTYR145
DTYR145

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q63470
ChainResidueDetails
ATYR219
BTYR219
CTYR219
DTYR219

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:23665168
ChainResidueDetails
ASER310
BSER310
CSER310
DSER310

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23665168
ChainResidueDetails
ATHR402
BTHR402
CTHR402
DTHR402

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AGLU291
AASP287

site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP287
BSER324
BLYS289

site_idCSA11
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP287
CSER324
CLYS289

site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DASP287
DSER324
DLYS289

site_idCSA13
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN292
AASP287
ALYS289

site_idCSA14
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN292
BASP287
BLYS289

site_idCSA15
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASN292
CASP287
CLYS289

site_idCSA16
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DASN292
DASP287
DLYS289

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BGLU291
BASP287

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CGLU291
CASP287

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DGLU291
DASP287

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP287
ALYS289

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP287
BLYS289

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP287
CLYS289

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DASP287
DLYS289

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP287
ASER324
ALYS289

223532

PDB entries from 2024-08-07

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