Structure of PDB 5tiu Chain A

Receptor sequence
>5tiuA (length=266) Species: 9606 (Homo sapiens) [Search protein sequence]
VYLDRKLLTLEDKELGTVKKGYYQMKKVVKTVAVKILKALKDELLAEANV
MQQLDNPYIVRMIGICEAESWMLVMEMAELGPLNKYLQQNRHVKDKNIIE
LVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADE
NYYKAQTHGKWPVKWYAPECINYYKFSSKSDVWSFGVLMWEAFSYGQKPY
RGMKGSEVTAMLEKGERMGCPAGCPREMYDLMNLCWTYDVENRPGFAAVE
LRLRNYYYDVVNEGHH
3D structure
PDB5tiu Carboxamide Spleen Tyrosine Kinase (Syk) Inhibitors: Leveraging Ground State Interactions To Accelerate Optimization.
ChainA
Resolution1.49 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) D494 A496 R498 N499 D512 K533
Catalytic site (residue number reindexed from 1) D121 A123 R125 N126 D139 K160
Enzyme Commision number 2.7.10.2: non-specific protein-tyrosine 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 7CU A L377 A400 M448 M450 A451 G454 P455 R498 L501 D512 L15 A33 M75 M77 A78 G81 P82 R125 L128 D139 MOAD: ic50=5nM
PDBbind-CN: -logKd/Ki=8.30,IC50=5nM
BindingDB: IC50=5.2nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5tiu, PDBe:5tiu, PDBj:5tiu
PDBsum5tiu
PubMed27994755
UniProtP43405|KSYK_HUMAN Tyrosine-protein kinase SYK (Gene Name=SYK)

[Back to BioLiP]