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6S11

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
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 Residues2
Detailsbinding site for residue CL A 501
ChainResidue
AHIS424
ALYS453

site_idAC2
Number of Residues14
Detailsbinding site for residue KQE A 502
ChainResidue
AGLU203
APHE238
AGLU239
ALEU241
ASER242
ALEU294
AASP307
AILE165
AGLY166
ALYS167
APHE170
AVAL173
AALA186
ALYS188

site_idAC3
Number of Residues12
Detailsbinding site for residue KQE B 501
ChainResidue
BILE165
BGLY166
BLYS167
BVAL173
BALA186
BLYS188
BGLU203
BPHE238
BGLU239
BLEU241
BLEU294
BASP307

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

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PDB entries from 2024-04-24

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