Crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 E60A mutant. Determined by X-ray diffraction at 1.55 Å resolution. Released 17 May 2005.
Explore 1Y34 in 3D Show helices and sheets RCSB PDB PDBe
1Y34 contains 13 α-helices and 28 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 1 |
| α-helix | 6-10 | 5 | |
| α-helix | 13-19 | 7 | |
| β-strand | 27-32 | 6 | 2 |
| β-strand | 44-49 | 6 | 2 |
| α-helix | 64-73 | 10 | |
| β-strand | 81 | 1 | 1 |
| β-strand | 89-94 | 6 | 2 |
| β-strand | 101-102 | 2 | 3 |
| α-helix | 104-116 | 13 | |
| β-strand | 121-124 | 4 | 2 |
| β-strand | 126-127 | 2 | 3 |
| β-strand | 128 | 1 | 4 |
| α-helix | 133-144 | 12 | |
| β-strand | 148-152 | 5 | 2 |
| β-strand | 167 | 1 | 4 |
| β-strand | 175-180 | 6 | 2 |
| α-helix | 185 | 1 | |
| β-strand | 186 | 1 | 2 |
| α-helix | 187 | 1 | |
| β-strand | 198-201 | 4 | 2 |
| β-strand | 205-209 | 5 | 5 |
| β-strand | 213-217 | 5 | 5 |
| β-strand | 219 | 1 | 6 |
| α-helix | 220-237 | 18 | |
| α-helix | 243-251 | 9 | |
| β-strand | 255 | 1 | 2 |
| α-helix | 260-263 | 4 | |
| β-strand | 267 | 1 | 2 |
| α-helix | 270-273 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 23 | 1 | 7 |
| α-helix | 25-27 | 3 | |
| β-strand | 31 | 1 | 8 |
| α-helix | 32-42 | 11 | |
| β-strand | 47-52 | 6 | 7 |
| β-strand | 56-58 | 3 | 3 |
| β-strand | 60 | 1 | 6 |
| β-strand | 65-70 | 6 | 7 |
| β-strand | 75 | 1 | 8 |
| β-strand | 76 | 1 | 7 |
| β-strand | 81-82 | 2 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| subtilisin BPN' | E | protein | 281 | Bacillus amyloliquefaciens | P00782 (AlphaFold model) |
| chymotrypsin inhibitor 2 | I | protein | 64 | Hordeum vulgare | Q40059 (AlphaFold model) |
>1Y34_1 subtilisin BPN' (chains E) AQSVPYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLKVAGGASMVPSETNPFQD NNSHGTHVAGTVAALNNSIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMD VINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSSTVGYPGKYPSVIAVGAV DSSNQRASFSSVGPELDVMAPGVSIQSTLPGNKYGAYNGTSMASPHVAGAAALILSKHPN WTNTQVRSSLENTTTKLGDSFYYGKGLINVQAAAQHHHHHH
>1Y34_2 chymotrypsin inhibitor 2 (chains I) MKTEWPELVGKSVEEAKKVILQDKPAAQIIVLPVGTIVTMAYRIDRVRLFVDRLDNIAQV PRVG
| ID | Name | Formula | Copies |
|---|---|---|---|
| 15P | Polyethylene glycol (N=34) | C69 H140 O35 | 4 |
| CIT | Citric acid | C6 H8 O7 | 3 |
| CA | Calcium ion | Ca | 1 |
Water and common crystallization additives (NA) are not listed.
Role of the intramolecular hydrogen bond network in the inhibitory power of chymotrypsin inhibitor 2. Radisky, E.S., Lu, C.J., Kwan, G. et al. Biochemistry (2005) 44:6823-6830. DOI 10.1021/bi047301w · PubMed
Other PDB entries of the same protein (UniProt P00782 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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