Research workbench
Crystal structure of glutamine synthetase from streptomyces coelicolor
Analyse Crystal structure of glutamine synthetase from streptomyces coelicolor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BAX
- Type
- protein
- Length
- 3,440 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamine synthetase
- EC
- 6.3.1.2
- UniProt
- Q9X958
- Ligands
- NA
- Pockets
- 20 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Glutamine synthetase (EC 6.3.1.2) | protein | 344 | 29% helix, 27% strand | Q9X958 |
Ligands and binding sites
- NA · Sodium ion · metal · 8 copies · chains A, B, C, D, E, F, J, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 863 | 0.76 | 0.79 | 81 | empty |
| 2 | 837 | 0.76 | 0.80 | 76 | empty |
| 3 | 702 | 0.76 | 0.81 | 76 | empty |
| 4 | 661 | 0.75 | 0.81 | 68 | empty |
| 5 | 706 | 0.75 | 0.81 | 69 | empty |
Interfaces
20 interfaces between chains.
- I–J · 1245 Ų buried · 27 hydrogen bonds · protein-protein
- F–G · 1212 Ų buried · 28 hydrogen bonds · protein-protein
- G–H · 1202 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 1200 Ų buried · 27 hydrogen bonds · protein-protein
- A–E · 1194 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 4BAX · Crystal structure of glutamine synthetase from Streptomyces coelicolor · 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 Q9X958
- Elsewhere: RCSB PDB 4BAX · PDBe 4BAX · UniProt Q9X958
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