Structure of PDB 4ith Chain A

Receptor sequence
>4ithA (length=247) Species: 9606 (Homo sapiens) [Search protein sequence]
NVIKMKSSDFLVSLAFHRTQGLMIMKTVNEALLEEAKMMNRLRHSRVVKL
LGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMAY
LHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLGTLYYMAPEH
LNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAIAEQQLIMAIKSGNRP
DVDDITEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYLSQLE
3D structure
PDB4ith Structural Basis of RIP1 Inhibition by Necrostatins.
ChainA
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D138 K140 E142 N143 D156 T189
Catalytic site (residue number reindexed from 1) D110 K112 E114 N115 D128 T142
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein 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 RCM A M67 L70 V75 V76 M92 H136 I154 A155 D156 S161 F162 M39 L42 V47 V48 M64 H108 I126 A127 D128 S133 F134 MOAD: ic50=0.3169uM
PDBbind-CN: -logKd/Ki=6.50,IC50=316.9nM
BindingDB: IC50=200nM,EC50=18nM
Gene Ontology
Molecular Function
GO:0004672 protein 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:4ith, PDBe:4ith, PDBj:4ith
PDBsum4ith
PubMed23473668
UniProtQ13546|RIPK1_HUMAN Receptor-interacting serine/threonine-protein kinase 1 (Gene Name=RIPK1)

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