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7KX6

Crystal structure of DCLK1-KD in complex with XMD8-85

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue X7Y A 701
ChainResidue
AILE396
AASP533
AHOH835
AHOH844
AGLU406
AALA417
AMET465
AGLU466
AVAL468
ALYS469
AGLU515
ALEU518

site_idAC2
Number of Residues12
Detailsbinding site for residue X7Y B 701
ChainResidue
BILE396
BGLU406
BVAL449
BMET465
BGLU466
BLEU467
BVAL468
BGLY471
BGLU515
BLEU518
BHOH805
BHOH822

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGDGNFAVVKeCverstareyalk......IIKK
ChainResidueDetails
AILE396-LYS423

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDIKpeNLLV
ChainResidueDetails
AILE507-VAL519

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
AASP511
BASP511

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BILE396
BLYS419
ALYS419
AILE396

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9JLM8
ChainResidueDetails
BSER376
ASER376

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9JLM8
ChainResidueDetails
BTYR520
ATYR520

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PDB entries from 2024-06-12

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