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6KYR

Crystal structure of DCLK1 mutant (P675L) Autoinhibited Kinase Domain

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 Residues3
Detailsbinding site for residue BME A 801
ChainResidue
AVAL547
ACYS548
ALYS692

site_idAC2
Number of Residues5
Detailsbinding site for residue BME A 802
ChainResidue
AARG442
ALEU505
AILE539
BGLY428
BHOH1017

site_idAC3
Number of Residues7
Detailsbinding site for Di-peptide BME B 801 and CYS B 548
ChainResidue
BTHR546
BVAL547
BGLY549
BVAL554
BHOH934
BHOH979
BMET432

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

239492

PDB entries from 2025-07-30

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