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4MQ1

The crystal structure of DYRK1a with a bound pyrido[2,3-d]pyrimidine 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 Residues19
DetailsBINDING SITE FOR RESIDUE 2C3 A 501
ChainResidue
AILE165
AGLU239
AMET240
ALEU241
ASER242
AASN292
ALEU294
AVAL306
AASP307
ASO4505
AHOH676
AGLY166
ALYS167
AGLY168
APHE170
AGLY171
AVAL173
ALYS188
APHE238

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 1PE A 502
ChainResidue
AASP162
ALYS175
ATRP184

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 1PE A 503
ChainResidue
AGLN201
CGLN201
CLEU234

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 504
ChainResidue
ATHR466
AARG467
AILE468
AGLN469
ATYR472

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 505
ChainResidue
AGLY168
ASER169
ALYS289
AGLY411
A2C3501
AHOH758
AHOH782

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 2C3 B 501
ChainResidue
BILE165
BLYS167
BGLY168
BGLY171
BGLN172
BLYS188
BPHE238
BGLU239
BMET240
BLEU241
BSER242
BTYR243
BASN292
BLEU294
BVAL306
BASP307
B1PE502
BHOH637
BHOH700
DGLN182

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 1PE B 502
ChainResidue
BASP162
BLYS175
BTRP184
B2C3501

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 1PE B 503
ChainResidue
BGLN201
BMET229
DGLN201

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 504
ChainResidue
BLYS264
BARG300
BSER301

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 505
ChainResidue
BARG467
BILE468
BGLN469
BTYR472

site_idBC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 2C3 C 501
ChainResidue
CILE165
CLYS167
CGLY168
CGLY171
CVAL173
CLYS188
CPHE238
CGLU239
CMET240
CLEU241
CSER242
CTYR243
CASN292
CLEU294
CVAL306
CASP307
C1PE502
CSO4503

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 1PE C 502
ChainResidue
CASP162
CLYS175
CTRP184
C2C3501
CHOH615

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 503
ChainResidue
CGLY168
CSER169
C2C3501
CHOH619

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 504
ChainResidue
CASN365
CGLU366
CLYS393
CPTR321

site_idBC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 2C3 D 501
ChainResidue
DILE165
DLYS167
DGLY168
DPHE170
DGLY171
DVAL173
DLYS188
DPHE238
DGLU239
DMET240
DLEU241
DSER242
DASN292
DLEU294
DASP307
D1PE502
DSO4503

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 1PE D 502
ChainResidue
DASP162
DLYS175
DTRP184
D2C3501
DHOH650
DHOH651

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 503
ChainResidue
DGLY168
DSER169
DLYS289
D2C3501

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 504
ChainResidue
DPTR321
DGLU366
DLYS393

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 Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:23665168
ChainResidueDetails
AASP287
BASP287
CASP287
DASP287

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
BLYS188
BPHE238
CILE165
CLYS188
CPHE238
DILE165
DLYS188
DPHE238
AILE165
ALYS188
APHE238
BILE165

site_idSWS_FT_FI3
Number of Residues24
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:23665168
ChainResidueDetails
APTR321
ATYR449
BTYR140
BTYR159
BTYR177
BTYR319
BPTR321
BTYR449
CTYR140
CTYR159
CTYR177
CTYR319
CPTR321
CTYR449
DTYR140
DTYR159
DTYR177
DTYR319
DPTR321
DTYR449
ATYR140
ATYR159
ATYR177
ATYR319

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
DTYR145
ATYR145
BTYR145
CTYR145

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q63470
ChainResidueDetails
ATYR219
BTYR219
CTYR219
DTYR219

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:23665168
ChainResidueDetails
BSER310
CSER310
DSER310
ASER310

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23665168
ChainResidueDetails
BTHR402
CTHR402
DTHR402
ATHR402

221051

PDB entries from 2024-06-12

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