Research workbench
Structure of gs-tnra complex
Analyse Structure of gs-tnra complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4S0R
- Type
- protein
- Length
- 6,416 residues
- Chains
- 28
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamine synthetase; Tnra peptide
- EC
- 6.3.1.2
- UniProt
- P12425
- Ligands
- GLN, MG
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 36% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, E, F, G, H, I, J, K, L, M, N | Glutamine synthetase (EC 6.3.1.2) | protein | 443 | 34% helix, 18% strand | P12425 |
| D | Glutamine synthetase (EC 6.3.1.2) | protein | 447 | 36% helix, 19% strand | P12425 |
| O, P, Q, R, S, T, U, V, W, X, Y, Z, 1, 2 | Tnra peptide | protein | 15 | 67% helix, 0% strand | — |
Ligands and binding sites
- GLN · Glutamine · ligand · 14 copies · chains A, B, N, C, E, D, F, G, M, H, I, J, K, L
- MG · Magnesium ion · metal · 47 copies · chains A, G, B, N, C, E, I, D, F, H, J, K, L, M
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 | 646 | 0.82 | 0.87 | 64 | empty |
| 2 | 411 | 0.81 | 0.90 | 60 | GLN, MG |
| 3 | 326 | 0.81 | 0.91 | 55 | GLN, MG |
| 4 | 418 | 0.81 | 0.89 | 52 | GLN, MG |
| 5 | 329 | 0.81 | 0.91 | 50 | GLN, MG |
Interfaces
76 interfaces between chains.
- B–D · 2167 Ų buried · 21 hydrogen bonds · protein-protein
- E–F · 2164 Ų buried · 21 hydrogen bonds · protein-protein
- L–M · 2160 Ų buried · 26 hydrogen bonds · protein-protein
- H–N · 2156 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 2141 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 4S0R · Structure of GS-TnrA complex · the same entry in another collection · chain B against B, 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 P12425
- Elsewhere: RCSB PDB 4S0R · PDBe 4S0R · UniProt P12425
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