Structure of PDB 5c27 Chain A

Receptor sequence
>5c27A (length=274) Species: 9606 (Homo sapiens) [Search protein sequence]
VYLDRKLLTLEDKELGSGNFGTVKKGYYQMKKVVKTVAVKILKNEANDPA
LKDELLAEANVMQQLDNPYIVRMIGICEAESWMLVMEMAELGPLNKYLQQ
NRHVKDKNIIELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISD
FGLSKALRADENYYKAQTHGKWPVKWYAPECINYYKFSSKSDVWSFGVLM
WEAFSYGQKPYRGMKGSEVTAMLEKGERMGCPAGCPREMYDLMNLCWTYD
VENRPGFAAVELRLRNYYYDVVNH
3D structure
PDB5c27 Imidazotriazines: Spleen Tyrosine Kinase (Syk) Inhibitors Identified by Free-Energy Perturbation (FEP).
ChainA
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D494 A496 R498 N499 D512 K533
Catalytic site (residue number reindexed from 1) D132 A134 R136 N137 D150 K171
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 peptide A D494 R498 G532 W534 P535 G578 D132 R136 G170 W172 P173 G216
BS02 50J A F382 V385 A400 V433 M448 M450 A451 E452 G454 P455 N457 Q461 L501 F20 V23 A38 V71 M86 M88 A89 E90 G92 P93 N95 Q99 L139
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

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Molecular Function
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Biological Process
External links
PDB RCSB:5c27, PDBe:5c27, PDBj:5c27
PDBsum5c27
PubMed26381330
UniProtP43405|KSYK_HUMAN Tyrosine-protein kinase SYK (Gene Name=SYK)

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