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2WO6

Human Dual-Specificity Tyrosine-Phosphorylation-Regulated Kinase 1A in complex with a consensus substrate peptide

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
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE D15 A 600
ChainResidue
AILE165
AASN292
ALEU294
AASP307
AHOH2191
AGLY168
AGLY171
AALA186
ALYS188
AGLU239
AMET240
ALEU241
ASER242

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE D15 B 600
ChainResidue
BILE165
BLYS167
BGLY168
BGLY171
BALA186
BLYS188
BGLU239
BMET240
BLEU241
BSER242
BASN292
BLEU294
BASP307
BCL700

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 700
ChainResidue
BLYS188
BD15600
BHOH2043

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:23665168
ChainResidueDetails
AASP287
BASP287

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AILE165
ALYS188
APHE238
BILE165
BLYS188
BPHE238

site_idSWS_FT_FI3
Number of Residues12
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:23665168
ChainResidueDetails
ATYR140
BTYR319
BPTR321
BTYR449
ATYR159
ATYR177
ATYR319
APTR321
ATYR449
BTYR140
BTYR159
BTYR177

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR145
BTYR145

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q63470
ChainResidueDetails
ATYR219
BTYR219

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:23665168
ChainResidueDetails
ASER310
BSER310

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23665168
ChainResidueDetails
ATHR402
BTHR402

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

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
AASP287
ALYS289

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP287
BLYS289

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP287
ASER324
ALYS289

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP287
BSER324
BLYS289

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN292
AASP287
ALYS289

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN292
BASP287
BLYS289

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PDB entries from 2024-10-09

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