Crystal structure of the complex of subtilisin bpn' with chymotrypsin inhibitor 2. Determined by X-ray diffraction at 1.7 Å resolution. Released 9 Nov 2004.
Explore 1TM1 in 3D Show helices and sheets RCSB PDB PDBe
1TM1 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 |
|---|---|---|---|
| α-helix | 6-10 | 5 | |
| α-helix | 13-19 | 7 | |
| β-strand | 27-32 | 6 | 1 |
| β-strand | 44-49 | 6 | 1 |
| α-helix | 64-73 | 10 | |
| β-strand | 89-94 | 6 | 1 |
| β-strand | 101-102 | 2 | 2 |
| α-helix | 104-116 | 13 | |
| β-strand | 121-124 | 4 | 1 |
| β-strand | 126-127 | 2 | 2 |
| β-strand | 128 | 1 | 3 |
| α-helix | 133-144 | 12 | |
| β-strand | 148-152 | 5 | 1 |
| β-strand | 159 | 1 | 4 |
| β-strand | 161 | 1 | 4 |
| β-strand | 167 | 1 | 3 |
| β-strand | 175-180 | 6 | 1 |
| α-helix | 185 | 1 | |
| β-strand | 186 | 1 | 1 |
| α-helix | 187 | 1 | |
| β-strand | 198-201 | 4 | 1 |
| 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 | 1 |
| α-helix | 260-263 | 4 | |
| β-strand | 267 | 1 | 1 |
| 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 | 2 |
| 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' precursor | E | protein | 281 | Bacillus amyloliquefaciens | P00782 (AlphaFold model) |
| chymotrypsin inhibitor 2 | I | protein | 64 | Hordeum vulgare subsp. vulgare | Q40059 (AlphaFold model) |
>1TM1_1 Subtilisin BPN' precursor (chains E) AQSVPYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLKVAGGASMVPSETNPFQD NNSHGTHVAGTVAALNNSIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMD VINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSSTVGYPGKYPSVIAVGAV DSSNQRASFSSVGPELDVMAPGVSIQSTLPGNKYGAYNGTSMASPHVAGAAALILSKHPN WTNTQVRSSLENTTTKLGDSFYYGKGLINVQAAAQHHHHHH
>1TM1_2 chymotrypsin inhibitor 2 (chains I) MKTEWPELVGKSVEEAKKVILQDKPAAQIIVLPVGTIVTMEYRIDRVRLFVDRLDNIAQV PRVG
Water and common crystallization additives (NA, 1PE) are not listed.
Binding, Proteolytic, and Crystallographic Analyses of Mutations at the Protease-Inhibitor Interface of the Subtilisin BPN'/Chymotrypsin Inhibitor 2 Complex(,). Radisky, E.S., Kwan, G., Karen Lu, C.J. et al. Biochemistry (2004) 43:13648-13656. DOI 10.1021/bi048797k · PubMed
Other PDB entries of the same protein (UniProt P00782 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1TM1 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.