Crystal structure of human chymotrypsin C (CTRC) bound to inhibitor eglin c from Hirudo medicinalis. Determined by X-ray diffraction at 1.9 Å resolution. Released 27 Feb 2013.
Explore 4H4F in 3D Show helices and sheets RCSB PDB PDBe
4H4F contains 14 α-helices and 33 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 | 17 | 1 | 1 |
| β-strand | 20-21 | 2 | 2 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-36A | 8 | 3 |
| β-strand | 37-48 | 12 | 3 |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 56-58 | 3 | |
| β-strand | 64-68 | 5 | 3 |
| β-strand | 72 | 1 | 4 |
| β-strand | 81-83 | 3 | 3 |
| β-strand | 85-90 | 6 | 3 |
| α-helix | 91 | 1 | |
| β-strand | 104-108 | 5 | 3 |
| α-helix | 111-114 | 4 | |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 2 |
| α-helix | 123-125 | 3 | |
| β-strand | 136-140 | 5 | 2 |
| β-strand | 143 | 1 | 5 |
| α-helix | 150 | 1 | |
| β-strand | 151 | 1 | 5 |
| α-helix | 152 | 1 | |
| β-strand | 154 | 1 | 4 |
| β-strand | 156-159 | 4 | 2 |
| β-strand | 162-163 | 2 | 2 |
| α-helix | 165-168 | 4 | |
| α-helix | 173-175 | 3 | |
| β-strand | 180-183 | 4 | 2 |
| β-strand | 189 | 1 | 1 |
| β-strand | 198-202 | 5 | 2 |
| β-strand | 207-216 | 10 | 2 |
| β-strand | 217 | 1 | 6 |
| β-strand | 219 | 1 | 6 |
| β-strand | 221A | 1 | 7 |
| β-strand | 224 | 1 | 7 |
| β-strand | 226-230 | 5 | 2 |
| α-helix | 231-233 | 3 | |
| α-helix | 235-241 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9 | 1 | 8 |
| α-helix | 11-13 | 3 | |
| β-strand | 17 | 1 | 8 |
| α-helix | 18-28 | 11 | |
| β-strand | 33-38 | 6 | 8 |
| β-strand | 43-44 | 2 | 2 |
| β-strand | 51-57 | 7 | 8 |
| β-strand | 62-63 | 2 | 8 |
| β-strand | 68-69 | 2 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chymotrypsin-C | A | protein | 249 | Homo sapiens | Q99895 (AlphaFold model) |
| Eglin C | B | protein | 70 | Hirudo medicinalis | P01051 (AlphaFold model) |
| Chymotrypsin-C | Q | protein | 10 | Homo sapiens | Q99895 (AlphaFold model) |
>4H4F_1 Chymotrypsin-C (chains A) VVGGEDARPHSWPWQISLQYLKNDTWRHTCGGTLIASNFVLTAAHCISNTRTYRVAVGKN NLEVEDEEGSLFVGVDTIHVHKRWNALLLRNDIALIKLAEHVELSDTIQVACLPEKDSLL PKDYPCYVTGWGRLWTNGPIADKLQQGLQPVVDHATCSRIDWWGFRVKKTMVCAGGDGVI SACNGDSGGPLNCQLENGSWEVFGIVSFGSRRGCNTRKKPVVYTRVSAYIDWINEKMQLH HHHHHHHHH
>4H4F_2 Eglin C (chains B) MSMGSELKSFPEVVGKTVDQAREYFTLHYPQYDVYFLPEGSPVTLDLRYNRVRVFYNPGT NVVNHVPHVG
>4H4F_3 Chymotrypsin-C (chains Q) CGVPSFPPNL
| ID | Name | Formula | Copies |
|---|---|---|---|
| PO4 | Phosphate ion | O4 P | 3 |
Long-range Electrostatic Complementarity Governs Substrate Recognition by Human Chymotrypsin C, a Key Regulator of Digestive Enzyme Activation. Batra, J., Szabo, A., Caulfield, T.R. et al. J Biol Chem (2013) 288:9848-9859. DOI 10.1074/jbc.M113.457382 · PubMed
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