Structure of PDB 2i0e Chain A

Receptor sequence
>2i0eA (length=329) Species: 9606 (Homo sapiens) [Search protein sequence]
LTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTM
VEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRF
KEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMC
KENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQ
APFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGP
EGERDIKEHAFFRYIDWEKLERKEIQPPYKPKACGRENFDRFFTRHPPVL
TPPDQEVIRNIDQSEFEGFSFVNSEFLKP
3D structure
PDB2i0e Structure of the Catalytic Domain of Human Protein Kinase C beta II Complexed with a Bisindolylmaleimide Inhibitor
ChainA
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D466 K468 D470 N471 D484 T504
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 PDS A L348 F353 V356 A369 T404 Y422 V423 D470 M473 A483 D484 L10 F15 V18 A31 T66 Y84 V85 D132 M135 A145 D146 PDBbind-CN: -logKd/Ki=8.70,Ki=2nM
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:2i0e, PDBe:2i0e, PDBj:2i0e
PDBsum2i0e
PubMed17115692
UniProtP05771|KPCB_HUMAN Protein kinase C beta type (Gene Name=PRKCB)

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