Structure of PDB 4ra5 Chain B

Receptor sequence
>4ra5B (length=312) Species: 9606 (Homo sapiens) [Search protein sequence]
LKIEDFELHKMLGKGSFGKVFLAEFKKTNQFFAIKALKKDVVLMDDDVEC
TMVEKRVLSLAWEHPFLTHMFCTFQTKENLFFVMEYLNGGDLMYHIQSCH
KFDLSRATFYAAEIILGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFG
MCKENMLGDAKTNEFCGTPDYIAPEILLGQKYNHSVDWWSFGVLLYEMLI
GQSPFHGQDEEELFHSIRMDNPFYPRWLEKEAKDLLVKLFVREPEKRLGV
RGDIRQHPLFREINWEELERKEIDPPFRPKVKSPFDPRLSRALINSMDQN
MFRNFSFMNPGM
3D structure
PDB4ra5 Optimized Protein Kinase C theta (PKC theta ) Inhibitors Reveal Only Modest Anti-inflammatory Efficacy in a Rodent Model of Arthritis.
ChainB
Resolution2.61 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) D504 K506 D508 N509 D522 T542
Catalytic site (residue number reindexed from 1) D130 K132 D134 N135 D148 T168
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 B G387 K388 V394 T442 M458 E459 L461 D508 D522 G13 K14 V20 T68 M84 E85 L87 D134 D148 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4ra5, PDBe:4ra5, PDBj:4ra5
PDBsum4ra5
PubMed25254961
UniProtQ04759|KPCT_HUMAN Protein kinase C theta type (Gene Name=PRKCQ)

[Back to BioLiP]