5LIH: Peptide-substrate

Structure of a peptide-substrate bound to PKCiota core kinase domain. Determined by X-ray diffraction at 3.25 Å resolution. Released 14 Sept 2016.

Method
X-ray diffraction
Resolution
3.25 Å
Organism
Homo sapiens
Chains
4
Atoms
5,298
Mol. weight
86.38 kDa
Ligands
ADP, AF3, MN, SCN
Released
14 Sept 2016

Explore 5LIH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5LIH contains 37 α-helices and 32 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 18 helices, 15 β-strands

ElementResiduesLengthSheet
α-helix251-2533
β-strand254-26291
β-strand266-27381
β-strand279-28681
α-helix301-3099
β-strand31512
α-helix316-3172
β-strand318-32361
β-strand327-33261
β-strand33912
α-helix342-3454
α-helix352-37019
β-strand37513
β-strand384-38632
β-strand392-39432
β-strand40113
β-strand41014
β-strand414-41525
α-helix422-4254
β-strand43014
α-helix433-44816
α-helix467-47610
α-helix478-4792
α-helix487-49610
α-helix512-5187
α-helix520-5223
α-helix527-5315
α-helix536-5372
α-helix546-5516
α-helix564-5663
α-helix571-5733
α-helix576-5783
β-strand584-58521
Chain B: 19 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix251-2533
β-strand254-26296
β-strand266-27386
β-strand279-28686
α-helix301-3099
β-strand31517
α-helix316-3172
β-strand318-32366
β-strand327-33266
β-strand33917
α-helix342-3454
α-helix352-37019
β-strand37518
α-helix381-3833
β-strand384-38637
β-strand392-39437
β-strand40118
β-strand41019
β-strand414-415210
α-helix422-4254
β-strand43019
α-helix433-44816
α-helix467-47610
α-helix478-4792
α-helix487-49610
α-helix512-5187
α-helix520-5234
α-helix527-5315
α-helix536-5372
α-helix546-5516
α-helix564-5663
α-helix571-5733
α-helix576-5783
β-strand584-58526
Chains F and G: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand12-1325

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein kinase C iota typeA, Bprotein349Homo sapiensP41743 (AlphaFold model)
PKC Epsilon pseudo substrate sequenceF, Gprotein16Homo sapiensQ02156 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5LIH_1 Protein kinase C iota type (chains A, B)
SLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQTEKHVFE
QASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALN
YLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRG
EDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSV
KAASVLKSFLNKDPKERLGCHPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFKPNISGEF
GLDNFDSQFTNEPVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV
Sequence of entity 2 (F, G), FASTA
>5LIH_2 PKC Epsilon pseudo substrate sequence (chains F, G)
ERMRPFKRQGSVRRRV

Ligands and cofactors

IDNameFormulaCopies
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P22
AF3Aluminum fluorideAl F34
MNManganese (II) ionMn5
SCNThiocyanate ionC N S2

Primary citation

aPKC Inhibition by Par3 CR3 Flanking Regions Controls Substrate Access and Underpins Apical-Junctional Polarization. Soriano, E.V., Ivanova, M.E., Fletcher, G. et al. Dev Cell (2016) 38:384-398. DOI 10.1016/j.devcel.2016.07.018 · PubMed

Other PDB entries of the same protein (UniProt P41743 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 5LIH directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.