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6S1B

Crystal Structure of DYRK1A with small molecule inhibitor

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
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue SO4 A 501
ChainResidue
ASER169
ALYS193
ALYS194
AHOH664
AHOH723
AHOH819
AHOH833

site_idAC2
Number of Residues9
Detailsbinding site for residue SO4 A 502
ChainResidue
ASER169
ALYS191
ALYS193
ALYS481
AHOH620
AHOH645
AHOH762
AASN144
AGLY168

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 A 503
ChainResidue
AARG325
AARG328
AGLU366
AHOH602
AHOH695
AHOH887

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 504
ChainResidue
ALYS264
AARG300
ASER301
AHOH836

site_idAC5
Number of Residues2
Detailsbinding site for residue SO4 A 505
ChainResidue
AARG226
AHOH629

site_idAC6
Number of Residues5
Detailsbinding site for residue SO4 A 506
ChainResidue
AASN365
AGLU366
AVAL367
ALYS393
AHOH768

site_idAC7
Number of Residues7
Detailsbinding site for residue KRQ A 507
ChainResidue
APHE170
AALA186
ALYS188
APHE238
AGLU239
ALEU241
AHOH697

site_idAC8
Number of Residues7
Detailsbinding site for residue EDO A 508
ChainResidue
ATHR466
AARG467
AILE468
AGLN469
ATYR472
AHOH609
AHOH864

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:23665168
ChainResidueDetails
AASP287

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AILE165
ALYS188
APHE238

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:23665168
ChainResidueDetails
ATYR140
ATYR159
ATYR177
ATYR319
APTR321
ATYR449

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR145

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q63470
ChainResidueDetails
ATYR219

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:23665168
ChainResidueDetails
ASER310

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23665168
ChainResidueDetails
ATHR402

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PDB entries from 2024-07-10

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