Research workbench
Complex between S. aureus aureolysin and impi mutant I57I
Analyse Complex between S. aureus aureolysin and impi mutant I57I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SKL
- Type
- protein
- Length
- 734 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Zinc metalloproteinase aureolysin; Impi alpha
- EC
- 3.4.24.29
- UniProt
- P81177, P82176
- Ligands
- CA, ZN
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 4 distinct chains · 35% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Zinc metalloproteinase aureolysin (EC 3.4.24.29) | protein | 301 | 44% helix, 19% strand | P81177 |
| B, D | Impi alpha | protein | 37 | 8% helix, 27% strand | P82176 |
| E | Impi alpha | protein | 30 | 10% helix, 40% strand | P82176 |
| F | Impi alpha | protein | 28 | 11% helix, 43% strand | P82176 |
Ligands and binding sites
- CA · Calcium ion · metal · 6 copies · chains A, C
- ZN · Zinc ion · metal · 2 copies · chains A, B, E, C, D, F
- EDO · 1,2-ethanediol · additive · 5 copies · chains A, B, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 959 | 0.79 | 0.81 | 87 | empty |
| 2 | 134 | 0.48 | 0.78 | 28 | empty |
| 3 | 139 | 0.42 | 0.75 | 23 | empty |
| 4 | 127 | 0.41 | 0.75 | 20 | empty |
| 5 | 53 | 0.35 | 0.79 | 17 | empty |
Interfaces
10 interfaces between chains.
- B–E · 1040 Ų buried · 34 hydrogen bonds · protein-protein
- D–F · 1001 Ų buried · 31 hydrogen bonds · protein-protein
- A–B · 633 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 626 Ų buried · 16 hydrogen bonds · protein-protein
- C–F · 436 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 7SKL · Complex between S. aureus aureolysin and IMPI mutant I57I · the same entry in another collection · chain F against F, TM-score 1.00
- P81177 · AlphaFold monomer V2.0 prediction for zinc metalloproteinase aureolysin (P81177) · a predicted model of the same protein · chain C against A, TM-score 0.99
- P82176 · AlphaFold monomer V2.0 prediction for inducible metalloproteinase inhibitor protein… · a predicted model of the same protein · chain E against A, TM-score 0.92
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P81177
- Every structure of UniProt P82176
- Elsewhere: RCSB PDB 7SKL · PDBe 7SKL · UniProt P81177 · UniProt P82176
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