Structure of PDB 1xjd Chain A

Receptor sequence
>1xjdA (length=282) Species: 9606 (Homo sapiens) [Search protein sequence]
IEDFILHKMLGKGSFGKVFLAEFKKTNQFFAIKALKKDVVLMDDDVECTM
VEKRVLSLAWEHPFLTHMFCTFQTKENLFFVMEYLNGGDLMYHIQSCHKF
DLSRATFYAAEIILGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMC
KENMLGDAKTNTFCGTPDYIAPEILLGQKYNHSVDWWSFGVLLYEMLIGQ
SPFHGQDEEELFHSIRMDNPFYPRWLEKEAKDLLVKLFVREPEKRLGVRG
DIRQHPLFREINWEELERKEIDPQNMFRNFSF
3D structure
PDB1xjd Catalytic domain crystal structure of protein kinase C-theta (PKCtheta)
ChainA
Resolution2.0 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) D128 K130 D132 N133 D146 T166
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 STU A L386 G387 K388 G389 V394 A407 M458 E459 Y460 L461 G464 D465 D508 N509 L511 D522 L10 G11 K12 G13 V18 A31 M82 E83 Y84 L85 G88 D89 D132 N133 L135 D146 MOAD: Ki=0.33nM
PDBbind-CN: -logKd/Ki=9.48,Ki=0.33nM
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:1xjd, PDBe:1xjd, PDBj:1xjd
PDBsum1xjd
PubMed15364937
UniProtQ04759|KPCT_HUMAN Protein kinase C theta type (Gene Name=PRKCQ)

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