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6N6O

Crystal structure of the human TTK in complex with an inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue KE7 A 801
ChainResidue
AILE531
ASER611
ALEU654
A1PE802
AGLN541
AALA551
AMET602
AGLU603
AGLY605
AASN606
AILE607
AASP608

site_idAC2
Number of Residues5
Detailsbinding site for residue 1PE A 802
ChainResidue
ALYS553
ATYR568
AGLU571
AMET600
AKE7801

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 803
ChainResidue
ALYS714
AGLN778
AARG779
AGLU784

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues23
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGGSSKVFqVlnekkqi...........YAIK
ChainResidueDetails
AILE531-LYS553

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHsDLKpaNFLI
ChainResidueDetails
AILE643-ILE655

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP647

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE531
ALYS553

227344

PDB entries from 2024-11-13

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