1ZRZ: Protein kinase C, iota

Crystal Structure of the Catalytic Domain of Atypical Protein Kinase C-iota. Determined by X-ray diffraction at 3.0 Å resolution. Released 13 Sept 2005.

Method
X-ray diffraction
Resolution
3.0 Å
Organism
Homo sapiens
Chains
1
Atoms
2,523
Mol. weight
42.41 kDa
Ligands
BI1
Released
13 Sept 2005

Explore 1ZRZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1ZRZ contains 19 α-helices and 15 β-strands across 1 chain. 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: 19 helices, 15 β-strands

ElementResiduesLengthSheet
β-strand245-25391
β-strand257-26481
β-strand270-27781
α-helix278-2803
α-helix287-29711
β-strand30612
β-strand309-31241
β-strand31411
β-strand318-32471
β-strand33012
α-helix331-3366
α-helix343-36220
β-strand36613
α-helix372-3743
β-strand375-37732
α-helix3781
β-strand383-38532
β-strand39213
β-strand40114
α-helix408-4103
α-helix413-4164
β-strand42114
α-helix424-43916
α-helix457-46711
α-helix469-4735
α-helix478-48710
α-helix503-5097
α-helix511-5133
α-helix518-5214
α-helix527-5282
α-helix553-5575
α-helix559-5624
α-helix568-5703
β-strand575-57621

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein kinase C, iotaAprotein364Homo sapiensP41743 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1ZRZ_1 Protein kinase C, iota (chains A)
EKEAMNTRESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVND
DEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPE
EHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTST
FCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQ
VILEKQIRIPRSMSVKAASVLKSFLNKDPKERLGCLPQTGFADIQGHPFFRNVDWDMMEQ
KQVVPPFKPNISGEFGLDNFDSQFTNERVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSA
EECV

Ligands and cofactors

IDNameFormulaCopies
BI13-{1-[3-(dimethylamino)propyl]-1H-indol-3-yl}-4-(1H-indol-3-yl)-1H-pyrrole-2,5-…C25 H24 N4 O21

Primary citation

Crystal Structure of the Catalytic Domain of Human Atypical Protein Kinase C-iota Reveals Interaction Mode of Phosphorylation Site in Turn Motif. Messerschmidt, A., Macieira, S., Velarde, M. et al. J Mol Biol (2005) 352:918-931. DOI 10.1016/j.jmb.2005.07.060 · PubMed

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

Browse structure collections

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