1CIQ: Chymotrypsin inhibitor 2

Complex of two fragments of CI2, residues 1-40 and 41-64. Determined by X-ray diffraction at 2.2 Å resolution. Released 8 Mar 1996.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Hordeum vulgare
Chains
2
Atoms
535
Mol. weight
7.33 kDa
Released
8 Mar 1996

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

Secondary structure: helices and β-sheets

1CIQ contains 2 α-helices and 7 β-strands across 2 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: 2 helices, 3 β-strands

ElementResiduesLengthSheet
β-strand411
α-helix6-83
β-strand1212
α-helix13-2311
β-strand28-3361
Chain B: 0 helices, 4 β-strands
ElementResiduesLengthSheet
β-strand46-5161
β-strand5612
β-strand5711
β-strand62-6321

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Chymotrypsin inhibitor 2Aprotein40Hordeum vulgareP01053 (AlphaFold model)
Chymotrypsin inhibitor 2Bprotein24Hordeum vulgareP01053 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1CIQ_1 CHYMOTRYPSIN INHIBITOR 2 (chains A)
MKTEWPELVGKSVEEAKKVILQDKPEAQIIVLPVGTIVTM
Sequence of entity 2 (B), FASTA
>1CIQ_2 CHYMOTRYPSIN INHIBITOR 2 (chains B)
EYRIDRVRLFVDKLDNIAQVPRVG

Primary citation

Towards the complete structural characterization of a protein folding pathway: the structures of the denatured, transition and native states for the association/folding of two complementary fragments of cleaved chymotrypsin inhibitor 2. Direct evidence for a nucleation-condensation mechanism. Neira, J.L., Davis, B., Ladurner, A.G. et al. Structure (1996) 1:189-208. DOI 10.1016/S1359-0278(96)00031-4 · PubMed

Other PDB entries of the same protein (UniProt P01053 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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