Research workbench
Cell wall binding domain of the staphylococcal phage 2638A endolysin
Analyse Cell wall binding domain of the staphylococcal phage 2638A endolysin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AQH
- Type
- protein
- Length
- 744 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ORF007
- UniProt
- Q4ZD58
- Pockets
- 8 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, C, G, H, B, E, F | ORF007 | protein | 93 | 0% helix, 56% strand | Q4ZD58 |
Ligands and binding sites
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A, H, E, D, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 371 | 0.62 | 0.78 | 37 | empty |
| 2 | 357 | 0.59 | 0.77 | 39 | empty |
| 3 | 109 | 0.41 | 0.76 | 18 | empty |
| 4 | 66 | 0.35 | 0.77 | 14 | empty |
| 5 | 58 | 0.32 | 0.75 | 12 | empty |
Interfaces
11 interfaces between chains.
- A–E · 493 Ų buried · 6 hydrogen bonds · protein-protein
- C–G · 490 Ų buried · 4 hydrogen bonds · protein-protein
- H–E · 488 Ų buried · 3 hydrogen bonds · protein-protein
- D–G · 476 Ų buried · 3 hydrogen bonds · protein-protein
- H–F · 474 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 7AQH · Cell wall binding domain of the Staphylococcal phage 2638A endolysin · the same entry in another collection · chain E against E, TM-score 1.00
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 Q4ZD58
- Elsewhere: RCSB PDB 7AQH · PDBe 7AQH · UniProt Q4ZD58
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