Structure of PDB 3hmo Chain A

Receptor sequence
>3hmoA (length=257) Species: 9606 (Homo sapiens) [Search protein sequence]
ANECISVKGRIYSILKQIGSGGSSKVFQVLNEKKQIYAIKYVNLEEADNQ
TLDSYRNEIAYLNKLQQHSDKIIRLYDYEITDQYIYMVMECGNIDLNSWL
KKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLI
DFGIANQMVGTVNYMPPEAIKDMISPKSDVWSLGCILYYMTYGKTPFQQI
INQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLA
HPYVQIQ
3D structure
PDB3hmo Biophysical and X-ray crystallographic analysis of Mps1 kinase inhibitor complexes.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) N556 L565 D647 K649 N652 D664 T686
Catalytic site (residue number reindexed from 1) N43 L52 D134 K136 N139 D151 T161
Enzyme Commision number 2.7.12.1: dual-specificity kinase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 STU A I531 G532 V539 A551 K553 C604 G605 N606 D608 L654 I18 G19 V26 A38 K40 C91 G92 N93 D95 L141 MOAD: Kd=30.5nM
PDBbind-CN: -logKd/Ki=7.52,Kd=30.5nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006468 protein phosphorylation

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3hmo, PDBe:3hmo, PDBj:3hmo
PDBsum3hmo
PubMed20099905
UniProtP33981|TTK_HUMAN Dual specificity protein kinase TTK (Gene Name=TTK)

[Back to BioLiP]