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4YU2

Crystal structure of DYRK1A with harmine-derivatized AnnH-75 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
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 Residues5
Detailsbinding site for residue PG4 A 501
ChainResidue
ALEU197
AGLN201
AMET229
CGLN201
CMET229

site_idAC2
Number of Residues7
Detailsbinding site for residue 4H5 A 502
ChainResidue
ALEU241
ALEU294
AASP307
APHE170
ALYS188
APHE238
AGLU239

site_idAC3
Number of Residues5
Detailsbinding site for residue PG4 B 501
ChainResidue
BGLN201
BHIS227
BMET229
DGLN201
DMET229

site_idAC4
Number of Residues11
Detailsbinding site for residue 4H5 B 502
ChainResidue
BILE165
BPHE170
BLYS188
BPHE238
BGLU239
BMET240
BLEU241
BLEU294
BASP307
BHOH617
BHOH618

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 B 503
ChainResidue
BPTR321
BARG325
BHOH625
DASN297

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 B 504
ChainResidue
BLYS264
BARG300
BSER301

site_idAC7
Number of Residues2
Detailsbinding site for residue SO4 B 505
ChainResidue
BGLU181
BARG226

site_idAC8
Number of Residues2
Detailsbinding site for residue PG4 C 501
ChainResidue
CTYR471
CTYR472

site_idAC9
Number of Residues11
Detailsbinding site for residue 4H5 C 502
ChainResidue
CPHE170
CVAL173
CLYS188
CVAL222
CPHE238
CGLU239
CMET240
CLEU241
CLEU294
CVAL306
CASP307

site_idAD1
Number of Residues3
Detailsbinding site for residue SO4 C 503
ChainResidue
CLYS264
CARG300
CSER301

site_idAD2
Number of Residues11
Detailsbinding site for residue 4H5 D 501
ChainResidue
DGLY166
DPHE170
DVAL173
DLYS188
DPHE238
DGLU239
DLEU241
DSER242
DLEU294
DASP307
DHOH619

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 Residues136
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues48
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues24
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q63470","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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