Crystal Structure of Cathepsin G Inhibited by Eap2 from S. aureus. Determined by X-ray diffraction at 1.85 Å resolution. Released 21 Dec 2022.
Explore 8D4V in 3D Show helices and sheets RCSB PDB PDBe
8D4V contains 26 α-helices and 64 β-strands across 4 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 | 30-36 | 7 | 3 |
| β-strand | 41-50 | 10 | 3 |
| β-strand | 53-56 | 4 | 3 |
| α-helix | 58-60 | 3 | |
| β-strand | 64-69 | 6 | 3 |
| β-strand | 73 | 1 | 4 |
| β-strand | 82-91 | 10 | 3 |
| β-strand | 96 | 1 | 5 |
| β-strand | 101 | 1 | 5 |
| β-strand | 105-109 | 5 | 3 |
| α-helix | 112-115 | 4 | |
| β-strand | 116 | 1 | 6 |
| β-strand | 119 | 1 | 6 |
| β-strand | 123 | 1 | 2 |
| α-helix | 124-125 | 2 | |
| β-strand | 136-141 | 6 | 2 |
| β-strand | 153 | 1 | 4 |
| β-strand | 155-161 | 7 | 2 |
| α-helix | 162-163 | 2 | |
| α-helix | 165-168 | 4 | |
| 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 | 158-165 | 8 | 3 |
| β-strand | 166 | 1 | 13 |
| β-strand | 169 | 1 | 13 |
| β-strand | 170-171 | 2 | 2 |
| β-strand | 174-179 | 6 | 3 |
| β-strand | 184-186 | 3 | 14 |
| α-helix | 187-202 | 16 | |
| α-helix | 206-211 | 6 | |
| β-strand | 216-221 | 6 | 3 |
| β-strand | 226-230 | 5 | 3 |
| β-strand | 240-242 | 3 | 14 |
| α-helix | 243-245 | 3 | |
| β-strand | 246-252 | 7 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 7 |
| β-strand | 20-21 | 2 | 8 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-36 | 7 | 9 |
| β-strand | 41-50 | 10 | 9 |
| β-strand | 53-56 | 4 | 9 |
| α-helix | 58-60 | 3 | |
| β-strand | 64-69 | 6 | 9 |
| β-strand | 73 | 1 | 10 |
| β-strand | 82-91 | 10 | 9 |
| β-strand | 96 | 1 | 11 |
| β-strand | 101 | 1 | 11 |
| β-strand | 105-109 | 5 | 9 |
| α-helix | 112-115 | 4 | |
| β-strand | 116 | 1 | 12 |
| β-strand | 119 | 1 | 12 |
| β-strand | 123 | 1 | 8 |
| α-helix | 124-125 | 2 | |
| β-strand | 136-141 | 6 | 8 |
| β-strand | 153 | 1 | 10 |
| β-strand | 155-161 | 7 | 8 |
| α-helix | 162-163 | 2 | |
| α-helix | 164-168 | 5 | |
| β-strand | 179-182 | 4 | 8 |
| β-strand | 190 | 1 | 7 |
| β-strand | 199-202 | 4 | 8 |
| β-strand | 205-213 | 9 | 8 |
| α-helix | 218 | 1 | |
| α-helix | 220 | 1 | |
| β-strand | 221-225 | 5 | 8 |
| α-helix | 226-229 | 4 | |
| α-helix | 230-237 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 157-165 | 9 | 9 |
| β-strand | 166 | 1 | 15 |
| β-strand | 169 | 1 | 15 |
| β-strand | 170-171 | 2 | 8 |
| β-strand | 174-180 | 7 | 9 |
| β-strand | 184-186 | 3 | 16 |
| α-helix | 187-202 | 16 | |
| α-helix | 206-211 | 6 | |
| β-strand | 216-221 | 6 | 9 |
| β-strand | 226-230 | 5 | 9 |
| β-strand | 240-242 | 3 | 16 |
| α-helix | 243-245 | 3 | |
| β-strand | 246-252 | 7 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cathepsin G, C-terminal truncated form | A, C | protein | 223 | Homo sapiens | P08311 (AlphaFold model) |
| Extracellular Adherence Protein | B, D | protein | 100 | Staphylococcus aureus subsp. aureus Mu50 | Q99QS1 (AlphaFold model) |
>8D4V_1 Cathepsin G, C-terminal truncated form (chains A, C) IIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQ RRENTQQHITARRAIRHPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGT LCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYDPRRQICVGDRRERKAAFKGD SGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMR
>8D4V_2 Extracellular Adherence Protein (chains B, D) GSTVQVPYTITVNGTSQNILSNLTFNKNQNISYKDLEGKVKSVLESNRGITDVDLRLSKQ AKYTVNFKNGTKKVIDLKSGIYTANLINSSDIKSININVD
Characterization of two distinct neutrophil serine protease-binding modes within a Staphylococcus aureus innate immune evasion protein family. Gido, C.D., Herdendorf, T.J., Geisbrecht, B.V. J Biol Chem (2023) 299:102969-102969. DOI 10.1016/j.jbc.2023.102969 · PubMed
Other PDB entries of the same protein (UniProt P08311 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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