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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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP275
BASP275

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AILE155
ALYS178
APHE228
BILE155
BLYS178
BPHE228

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by MAP3K10 => ECO:0000269|PubMed:18455992
ChainResidueDetails
ATHR308
BTHR308

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:22998443
ChainResidueDetails
APTR309
BPTR309

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by ATM => ECO:0000269|PubMed:19965871
ChainResidueDetails
ASER369
BSER369

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by MAP3K10 => ECO:0000269|PubMed:18455992
ChainResidueDetails
ASER376
BSER376

222415

PDB entries from 2024-07-10

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