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The crystal structure of glutamine synthetase from bifidobacterium adolescentis atcc 15703
Analyse The crystal structure of glutamine synthetase from bifidobacterium adolescentis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4S17
- Type
- protein
- Length
- 2,699 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamine synthetase
- EC
- 6.3.1.2
- UniProt
- A1A1Z1
- Ligands
- MG
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 6 distinct chains · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamine synthetase (EC 6.3.1.2) | protein | 452 | 35% helix, 24% strand | A1A1Z1 |
| B | Glutamine synthetase (EC 6.3.1.2) | protein | 451 | 35% helix, 24% strand | A1A1Z1 |
| C | Glutamine synthetase (EC 6.3.1.2) | protein | 447 | 35% helix, 23% strand | A1A1Z1 |
| D | Glutamine synthetase (EC 6.3.1.2) | protein | 450 | 34% helix, 24% strand | A1A1Z1 |
| E | Glutamine synthetase (EC 6.3.1.2) | protein | 450 | 36% helix, 24% strand | A1A1Z1 |
| F | Glutamine synthetase (EC 6.3.1.2) | protein | 449 | 34% helix, 25% strand | A1A1Z1 |
Ligands and binding sites
- MG · Magnesium ion · metal · 6 copies · chains A, B, C, D, E, F
- ACT · Acetate ion · additive · 2 copies · chains B, C
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 | 1032 | 0.78 | 0.79 | 64 | empty |
| 2 | 1067 | 0.78 | 0.80 | 75 | empty |
| 3 | 1119 | 0.77 | 0.79 | 71 | empty |
| 4 | 1088 | 0.77 | 0.79 | 73 | empty |
| 5 | 1089 | 0.77 | 0.79 | 74 | empty |
Interfaces
6 interfaces between chains.
- B–C · 1645 Ų buried · 29 hydrogen bonds · protein-protein
- A–F · 1623 Ų buried · 34 hydrogen bonds · protein-protein
- C–D · 1621 Ų buried · 33 hydrogen bonds · protein-protein
- A–B · 1615 Ų buried · 29 hydrogen bonds · protein-protein
- D–E · 1601 Ų buried · 34 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 54 modified (engineered).
Compared structures
- 4S17 · The crystal structure of glutamine synthetase from Bifidobacterium adolescentis ATCC 15703 · 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 A1A1Z1
- Elsewhere: RCSB PDB 4S17 · PDBe 4S17 · UniProt A1A1Z1
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