Research workbench
Crystal structure of mouse glutaminase C, phosphate-bound form
Analyse Crystal structure of mouse glutaminase C, phosphate-bound form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SS4
- Type
- protein
- Length
- 1,559 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutaminase C
- EC
- 3.5.1.2
- UniProt
- Q69ZX9
- Ligands
- PO4
- Pockets
- 9 · best druggability 0.75
Structure
x-ray diffraction · 4 distinct chains · 50% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutaminase C (EC 3.5.1.2) | protein | 390 | 51% helix, 12% strand | Q69ZX9 |
| B | Glutaminase C (EC 3.5.1.2) | protein | 388 | 50% helix, 11% strand | Q69ZX9 |
| C | Glutaminase C (EC 3.5.1.2) | protein | 394 | 49% helix, 10% strand | Q69ZX9 |
| D | Glutaminase C (EC 3.5.1.2) | protein | 387 | 49% helix, 11% strand | Q69ZX9 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1033 | 0.75 | 0.78 | 110 | PO4 |
| 2 | 1028 | 0.75 | 0.77 | 102 | PO4 |
| 3 | 308 | 0.70 | 0.84 | 34 | empty |
| 4 | 372 | 0.69 | 0.82 | 47 | empty |
| 5 | 54 | 0.35 | 0.79 | 12 | empty |
Interfaces
4 interfaces between chains.
- A–C · 1725 Ų buried · 29 hydrogen bonds · protein-protein
- B–D · 1708 Ų buried · 25 hydrogen bonds · protein-protein
- B–C · 531 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 523 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3SS4 · Crystal structure of mouse Glutaminase C, phosphate-bound form · 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 Q69ZX9
- Elsewhere: RCSB PDB 3SS4 · PDBe 3SS4 · UniProt Q69ZX9
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