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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
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_FI2
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9JLM8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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