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5LXD

Crystal structure of DYRK2 in complex with EHT 1610 (compound 2)

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 Residues13
Detailsbinding site for residue 7A7 A 501
ChainResidue
AGLY156
ALEU231
ALEU282
AILE294
AASP295
ALYS157
APHE160
AVAL163
AALA176
ALYS178
AILE212
APHE228
AGLU229

site_idAC2
Number of Residues1
Detailsbinding site for residue EDO A 502
ChainResidue
AASN381

site_idAC3
Number of Residues2
Detailsbinding site for residue EDO A 503
ChainResidue
AARG421
AASN425

site_idAC4
Number of Residues1
Detailsbinding site for residue EDO A 504
ChainResidue
AARG458

site_idAC5
Number of Residues2
Detailsbinding site for residue EDO A 505
ChainResidue
AARG288
AGLY290

site_idAC6
Number of Residues3
Detailsbinding site for residue EDO A 506
ChainResidue
ASER384
ASER385
AARG390

site_idAC7
Number of Residues14
Detailsbinding site for residue 7A7 B 501
ChainResidue
BGLY156
BLYS157
BPHE160
BVAL163
BALA176
BLYS178
BILE212
BPHE228
BGLU229
BLEU231
BASN280
BLEU282
BILE294
BASP295

site_idAC8
Number of Residues1
Detailsbinding site for residue EDO B 502
ChainResidue
BTHR308

site_idAC9
Number of Residues2
Detailsbinding site for residue EDO B 503
ChainResidue
BARG378
BASN381

site_idAD1
Number of Residues3
Detailsbinding site for residue EDO B 504
ChainResidue
BARG421
BASN425
BHOH642

site_idAD2
Number of Residues2
Detailsbinding site for residue EDO B 505
ChainResidue
BARG288
BGLY290

site_idAD3
Number of Residues3
Detailsbinding site for residue EDO B 506
ChainResidue
BSER384
BSER385
BARG390

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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