Human Cathepsin-G Inhibited by S. aureus EapH1. Determined by X-ray diffraction at 1.6 Å resolution. Released 22 Apr 2020.
Explore 6VTM in 3D Show helices and sheets RCSB PDB PDBe
6VTM contains 46 α-helices and 128 β-strands across 8 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 | 30-37 | 8 | 3 |
| β-strand | 40-50 | 11 | 3 |
| β-strand | 53-56 | 4 | 3 |
| α-helix | 58-60 | 3 | |
| β-strand | 65-69 | 5 | 3 |
| β-strand | 73 | 1 | 4 |
| β-strand | 76 | 1 | 5 |
| β-strand | 82-91 | 10 | 3 |
| β-strand | 96 | 1 | 6 |
| β-strand | 101 | 1 | 6 |
| β-strand | 105-109 | 5 | 3 |
| β-strand | 116 | 1 | 7 |
| β-strand | 119 | 1 | 7 |
| β-strand | 123 | 1 | 2 |
| α-helix | 124-126 | 3 | |
| β-strand | 136-141 | 6 | 2 |
| β-strand | 153 | 1 | 4 |
| β-strand | 155-161 | 7 | 2 |
| α-helix | 162-163 | 2 | |
| α-helix | 164-170 | 7 | |
| β-strand | 179-182 | 4 | 2 |
| β-strand | 190 | 1 | 1 |
| β-strand | 199-202 | 4 | 2 |
| β-strand | 205-213 | 9 | 2 |
| α-helix | 218 | 1 | |
| α-helix | 220 | 1 | |
| β-strand | 221-225 | 5 | 2 |
| α-helix | 226-229 | 4 | |
| α-helix | 230-237 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 45-53 | 9 | 3 |
| β-strand | 56 | 1 | 3 |
| β-strand | 57-58 | 2 | 2 |
| β-strand | 61-66 | 6 | 3 |
| β-strand | 72-73 | 2 | 8 |
| α-helix | 74-89 | 16 | |
| α-helix | 93-98 | 6 | |
| β-strand | 102-108 | 7 | 3 |
| β-strand | 113-117 | 5 | 3 |
| β-strand | 127-128 | 2 | 8 |
| α-helix | 130-132 | 3 | |
| β-strand | 133-140 | 8 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 15 |
| β-strand | 20-21 | 2 | 16 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-37 | 8 | 17 |
| β-strand | 40-50 | 11 | 17 |
| β-strand | 53-56 | 4 | 17 |
| α-helix | 58-60 | 3 | |
| β-strand | 65-69 | 5 | 17 |
| β-strand | 73 | 1 | 18 |
| β-strand | 82-91 | 10 | 17 |
| β-strand | 96 | 1 | 19 |
| β-strand | 101 | 1 | 19 |
| β-strand | 105-109 | 5 | 17 |
| β-strand | 116 | 1 | 20 |
| β-strand | 119 | 1 | 20 |
| β-strand | 123 | 1 | 21 |
| α-helix | 124-126 | 3 | |
| β-strand | 136-141 | 6 | 16 |
| β-strand | 146 | 1 | 22 |
| β-strand | 149 | 1 | 22 |
| β-strand | 153 | 1 | 18 |
| β-strand | 155-161 | 7 | 16 |
| α-helix | 164-170 | 7 | |
| β-strand | 179-182 | 4 | 16 |
| β-strand | 190 | 1 | 15 |
| β-strand | 199-201 | 3 | 16 |
| β-strand | 205 | 1 | 21 |
| β-strand | 206-213 | 8 | 16 |
| β-strand | 221-225 | 5 | 16 |
| α-helix | 226-229 | 4 | |
| α-helix | 230-237 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 25 |
| β-strand | 20-21 | 2 | 26 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-37 | 8 | 27 |
| β-strand | 40-50 | 11 | 27 |
| β-strand | 53-56 | 4 | 27 |
| α-helix | 58-60 | 3 | |
| β-strand | 65-69 | 5 | 27 |
| β-strand | 73 | 1 | 28 |
| β-strand | 82-91 | 10 | 27 |
| β-strand | 96 | 1 | 29 |
| β-strand | 101 | 1 | 29 |
| β-strand | 105-109 | 5 | 27 |
| β-strand | 116 | 1 | 30 |
| β-strand | 119 | 1 | 30 |
| α-helix | 125-126 | 2 | |
| β-strand | 136-141 | 6 | 26 |
| β-strand | 153 | 1 | 28 |
| β-strand | 155-161 | 7 | 26 |
| α-helix | 162-163 | 2 | |
| α-helix | 164-170 | 7 | |
| β-strand | 179-182 | 4 | 26 |
| β-strand | 190 | 1 | 25 |
| α-helix | 198 | 1 | |
| β-strand | 199-202 | 4 | 26 |
| β-strand | 205-213 | 9 | 26 |
| α-helix | 218 | 1 | |
| α-helix | 220 | 1 | |
| β-strand | 221-225 | 5 | 26 |
| α-helix | 226-229 | 4 | |
| α-helix | 230-237 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cathepsin G | A, C, D, G | protein | 224 | Homo sapiens | P08311 (AlphaFold model) |
| MAP domain-containing protein | B, E, F, H | protein | 99 | Staphylococcus aureus (strain Mu50 / ATCC 700699) | A0A0H3K0M1 (AlphaFold model) |
>6VTM_1 Cathepsin G (chains A, C, D, G) IIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQ RRENTQQHITARRAIRHPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGT LCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYDPRRQICVGDRRERKAAFKGD SGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMRS
>6VTM_2 MAP domain-containing protein (chains B, E, F, H) GKHTVPYTISVDGITALHRTYFVFPENKKVLYQEIDSKVKNELASQRGVTTEKINNAQTA TYTLTLNDGNKKVVNLKKNDDAKNSIDPSTIKQIQIVVK
Crystal Structure of Human Cathepsin-G Inhibited by S. aureus EapH1. Herdendorf, T.J., Rooijakkers, S.H.M., Geisbrecht, B.V. J Biol Chem (2020).
Other PDB entries of the same protein (UniProt P08311 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 6VTM 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.