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5LXC

Crystal structure of DYRK2 in complex with EHT 5372 (Compound 1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004712molecular_functionprotein serine/threonine/tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004712molecular_functionprotein serine/threonine/tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue 7AA A 501
ChainResidue
AILE155
ALEU231
ASER232
AASN234
AGLU279
ALEU282
AILE294
AEDO504
AGLY156
ALYS157
AVAL163
AALA176
ALYS178
AILE212
APHE228
AGLU229

site_idAC2
Number of Residues2
Detailsbinding site for residue EDO A 502
ChainResidue
ALYS165
AHOH654

site_idAC3
Number of Residues3
Detailsbinding site for residue EDO A 503
ChainResidue
AGLU363
ALYS413
AARG415

site_idAC4
Number of Residues7
Detailsbinding site for residue EDO A 504
ChainResidue
AILE155
ASER232
AMET233
AASN234
A7AA501
AHOH699
AHOH710

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 506
ChainResidue
AHIS199
ALYS202
BASP437
BGLN441

site_idAC6
Number of Residues1
Detailsbinding site for residue EDO A 507
ChainResidue
ALYS254

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO A 508
ChainResidue
APRO350
ALYS413
AARG415
BARG411

site_idAC8
Number of Residues3
Detailsbinding site for residue EDO A 509
ChainResidue
ASER104
ATYR105
AHOH633

site_idAC9
Number of Residues16
Detailsbinding site for residue 7AA B 501
ChainResidue
BILE155
BGLY156
BLYS157
BPHE160
BVAL163
BALA176
BLYS178
BILE212
BPHE228
BGLU229
BLEU231
BGLU279
BLEU282
BILE294
BASP295
BHOH673

site_idAD1
Number of Residues5
Detailsbinding site for residue EDO B 502
ChainResidue
ALYS202
BLEU436
BLYS440
BHOH646
BHOH719

site_idAD2
Number of Residues5
Detailsbinding site for residue EDO B 503
ChainResidue
BLYS277
BGLU279
BSER312
BHOH605
BHOH643

site_idAD3
Number of Residues2
Detailsbinding site for residue EDO B 504
ChainResidue
BLYS386
BTYR388

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSFGQVVkAydhkvhqh..........VALK
ChainResidueDetails
AILE155-LYS178

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHcDLKpeNILL
ChainResidueDetails
AILE271-LEU283

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"source":"PubMed","id":"19965871","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by MAP3K10","evidences":[{"source":"PubMed","id":"18455992","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"22998443","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by ATM","evidences":[{"source":"PubMed","id":"19965871","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by MAP3K10","evidences":[{"source":"PubMed","id":"18455992","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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