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6A1F

Crystal structure of human DYRK1A in complex with compound 14

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 Residues5
Detailsbinding site for residue SO4 A 801
ChainResidue
ALYS167
APHE479
ALYS480
ALYS481
AHOH1030

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 802
ChainResidue
ALYS264
AARG300
ASER301
AHOH1038

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 803
ChainResidue
AASN365
AGLU366
AVAL367
ALYS393

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 804
ChainResidue
ASER169
ALYS193
ALYS194
AHOH969

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 A 805
ChainResidue
AASN232
AARG325
AARG328
AGLU366

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 A 806
ChainResidue
AARG226
AHOH940
AHOH1041

site_idAC7
Number of Residues9
Detailsbinding site for residue 9OF A 807
ChainResidue
ALYS167
APHE170
AVAL173
AALA186
APHE238
AGLU239
ALEU241
ALEU294
APGE808

site_idAC8
Number of Residues11
Detailsbinding site for residue PGE A 808
ChainResidue
ALYS188
AGLU203
APHE238
AASN244
AGLU291
AASN292
ALEU294
AVAL306
AASP307
A9OF807
AHOH921

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
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q63470","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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