2CI2: Chymotrypsin inhibitor 2

Crystal and molecular structure of the serine proteinase inhibitor ci-2 from barley seeds. Determined by X-ray diffraction at 2.0 Å resolution. Released 7 Sept 1988.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Hordeum vulgare
Chains
1
Atoms
585
Mol. weight
9.26 kDa
Released
7 Sept 1988

Explore 2CI2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2CI2 contains 3 α-helices and 7 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 I: 3 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand2311
α-helix25-273
β-strand3112
α-helix32-4211
β-strand47-5261
α-helix55-584
β-strand65-7061
β-strand7512
β-strand7611
β-strand81-8221

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Chymotrypsin inhibitor 2Iprotein83Hordeum vulgareP01053 (AlphaFold model)
Sequence of entity 1 (I), FASTA
>2CI2_1 CHYMOTRYPSIN INHIBITOR 2 (chains I)
SSVEKKPEGVNTGAGDRHNLKTEWPELVGKSVEEAKKVILQDKPEAQIIVLPVGTIVTME
YRIDRVRLFVDKLDNIAEVPRVG

Primary citation

Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds. McPhalen, C.A., James, M.N. Biochemistry (1987) 26:261-269. DOI 10.1021/bi00375a036 · 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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