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5JZN

Crystal structure of DCLK1-KD in complex with NVP-TAE684

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 Residues10
Detailsbinding site for residue GUI A 701
ChainResidue
AILE396
ALEU518
AVAL404
ALYS419
AGLU466
AVAL468
AGLY471
AASP475
AGLU515
AASN516

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 702
ChainResidue
AARG510
ATHR546
BARG510
BTHR546

site_idAC3
Number of Residues11
Detailsbinding site for residue GUI B 701
ChainResidue
BILE396
BGLU406
BLYS419
BGLU466
BLEU467
BVAL468
BGLY471
BASP475
BGLU515
BASN516
BLEU518

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
AILE396
ALYS419

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

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

221051

PDB entries from 2024-06-12

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