Structure of PDB 4ra5 Chain A

Receptor sequence
>4ra5A (length=334) Species: 9606 (Homo sapiens) [Search protein sequence]
KLKIEDFELHKMLGKGSFGKVFLAEFKKTNQFFAIKALKKDVVLMDDDVE
CTMVEKRVLSLAWEHPFLTHMFCTFQTKENLFFVMEYLNGGDLMYHIQSC
HKFDLSRATFYAAEIILGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADF
GMCKENMLGDAKTNEFCGTPDYIAPEILLGQKYNHSVDWWSFGVLLYEML
IGQSPFHGQDEEELFHSIRMDNPFYPRWLEKEAKDLLVKLFVREPEKRLG
VRGDIRQHPLFREINWEELERKEIDPPFRPKVKSPFDCSNFDKEFLNEKP
RLSFADRALINSMDQNMFRNFSFMNPGMERLISH
3D structure
PDB4ra5 Optimized Protein Kinase C theta (PKC theta ) Inhibitors Reveal Only Modest Anti-inflammatory Efficacy in a Rodent Model of Arthritis.
ChainA
Resolution2.61 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D504 K506 D508 N509 D522 T542
Catalytic site (residue number reindexed from 1) D131 K133 D135 N136 D149 T169
Enzyme Commision number 2.7.11.13: protein kinase C.
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 3L0 A L386 G387 K388 V394 A407 M458 E459 D508 L511 D522 F664 F668 L13 G14 K15 V21 A34 M85 E86 D135 L138 D149 F291 F295 PDBbind-CN: -logKd/Ki=8.40,IC50=4nM
BindingDB: IC50=4.0nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0004697 diacylglycerol-dependent serine/threonine 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:4ra5, PDBe:4ra5, PDBj:4ra5
PDBsum4ra5
PubMed25254961
UniProtQ04759|KPCT_HUMAN Protein kinase C theta type (Gene Name=PRKCQ)

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