Research workbench
Crystal structure of salmonella typhimurium apha protein
Analyse Crystal structure of salmonella typhimurium apha protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z5G
- Type
- protein
- Length
- 835 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Apha protein
- EC
- 3.1.3.2
- UniProt
- Q5MB24
- Ligands
- MG, PO4
- Pockets
- 11 · best druggability 0.72
Structure
x-ray diffraction · 3 distinct chains · 37% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Apha protein (EC 3.1.3.2) | protein | 208 | 37% helix, 17% strand | Q5MB24 |
| B | Apha protein (EC 3.1.3.2) | protein | 209 | 37% helix, 17% strand | Q5MB24 |
| D | Apha protein (EC 3.1.3.2) | protein | 210 | 37% helix, 17% strand | Q5MB24 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 561 | 0.72 | 0.80 | 67 | empty |
| 2 | 300 | 0.65 | 0.81 | 42 | PO4 |
| 3 | 303 | 0.58 | 0.77 | 41 | empty |
| 4 | 211 | 0.54 | 0.79 | 28 | MG |
| 5 | 227 | 0.54 | 0.78 | 27 | MG |
Interfaces
6 interfaces between chains.
- A–B · 1377 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 1354 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 1007 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 991 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 643 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 1Z5G · Crystal structure of Salmonella typhimurium AphA protein · the same entry in another collection · chain A against A, 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 Q5MB24
- Elsewhere: RCSB PDB 1Z5G · PDBe 1Z5G · UniProt Q5MB24
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