Structure of PDB 1zrz Chain A

Receptor sequence
>1zrzA (length=312) Species: 9606 (Homo sapiens) [Search protein sequence]
LGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDW
VQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQR
KLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYG
MCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMA
GRSPFDQNTEDYLFQVILEKQIRIPRSMSVKAASVLKSFLNKDPKERLGC
LPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFKPVQLTPDDDDIVRKIDQ
SEFEGFEYINPL
3D structure
PDB1zrz Crystal Structure of the Catalytic Domain of Human Atypical Protein Kinase C-iota Reveals Interaction Mode of Phosphorylation Site in Turn Motif
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D369 K371 N374 D387 T407
Catalytic site (residue number reindexed from 1) D130 K132 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 BI1 A I251 G252 V259 A272 K274 E324 Y325 V326 D373 L376 T386 D387 I12 G13 V20 A33 K35 E85 Y86 V87 D134 L137 T147 D148 PDBbind-CN: -logKd/Ki=5.24,IC50=5.8uM
BindingDB: IC50=3463nM
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:1zrz, PDBe:1zrz, PDBj:1zrz
PDBsum1zrz
PubMed16125198
UniProtP41743|KPCI_HUMAN Protein kinase C iota type (Gene Name=PRKCI)

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