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6UIP

DYRK1A Kinase Domain in Complex with a 6-azaindole Derivative, GNF2133.

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
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue Q8J A 501
ChainResidue
AILE165
AALA186
ALYS188
AGLU239
ALEU241
AASN292
ALEU294
AVAL306
AASP307

site_idAC2
Number of Residues10
Detailsbinding site for residue Q8J B 501
ChainResidue
BILE165
BLYS188
BPHE238
BGLU239
BMET240
BLEU241
BTYR243
BASN292
BLEU294
BVAL306

site_idAC3
Number of Residues8
Detailsbinding site for residue Q8J C 501
ChainResidue
CALA186
CLYS188
CGLU239
CLEU241
CASN292
CLEU294
CVAL306
CASP307

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 Residues3
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
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 Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q63470","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues34
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

250059

PDB entries from 2026-03-04

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