Structure of PDB 2jed Chain A

Receptor sequence
>2jedA (length=326) Species: 9606 (Homo sapiens) [Search protein sequence]
LKIEDFELHKMLGKGSFGKVFLAEFKKTNQFFAIKALKKDVVLMDDDVEC
TMVEKRVLSLAWEHPFLTHMFCTFQTKENLFFVMEYLNGGDLMYHIQSCH
KFDLSRATFYAAEIILGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFG
MCKENMLGDAKTNEFCGTPDYIAPEILLGQKYNHSVDWWSFGVLLYEMLI
GQSPFHGQDEEELFHSIRMDNPFYPRWLEKEAKDLLVKLFVREPEKRLGV
RGDIRQHPLFREINWEELERKEIDPPFRPKVKSPFDCSNFDKEFLNEKPR
LSFADRALINSMDQNMFRNFSFMNPG
3D structure
PDB2jed Improved Expression of Kinases in Baculovirus-Infected Insect Cells Upon Addition of Specific Kinase Inhibitors to the Culture Helpful for Structural Studies.
ChainA
Resolution2.32 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) 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 LG8 A L386 G387 F391 V394 A407 K409 T442 E459 L461 D465 L511 D522 F664 L12 G13 F17 V20 A33 K35 T68 E85 L87 D91 L137 D148 F290
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:2jed, PDBe:2jed, PDBj:2jed
PDBsum2jed
PubMed
UniProtQ04759|KPCT_HUMAN Protein kinase C theta type (Gene Name=PRKCQ)

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