MolNFT v1 · #50939 · protein
Thermotoga maritima glutamate dehydrogenase mutant S128R, T158E, N117R, S160E
2TMG · Protein (glutamate dehydrogenase): “Thermotoga maritima glutamate dehydrogenase mutant S128R, T158E, N117R, S160E”. X-ray diffraction, 18 pockets (best druggability 0.87). MolNFT v1 #50939 on GenesisL1: 3D structure, binding sites…
- PDB
- 2TMG
- Type
- protein
- Length
- 2,448 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (glutamate dehydrogenase)
- EC
- 1.4.1.3
- UniProt
- P96110
- Pockets
- 18 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Protein (glutamate dehydrogenase) (EC 1.4.1.3) | protein | 408 | 48% helix, 17% strand | P96110 |
Pockets
18 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1150 | 0.87 | 0.89 | 95 | empty |
| 2 | 1159 | 0.87 | 0.89 | 99 | empty |
| 3 | 1137 | 0.87 | 0.88 | 96 | empty |
| 4 | 807 | 0.77 | 0.81 | 98 | empty |
| 5 | 963 | 0.75 | 0.78 | 97 | empty |
Interfaces
12 interfaces between chains.
- A–F · 974 Ų buried · 16 hydrogen bonds · protein-protein
- B–E · 971 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 958 Ų buried · 14 hydrogen bonds · protein-protein
- E–F · 825 Ų buried · 10 hydrogen bonds · protein-protein
- D–F · 821 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 2TMG · Thermotoga maritima glutamate dehydrogenase mutant S128R, T158E, N117R, S160E · the same entry in another collection · chain F against F, TM-score 1.00
- P96110 · AlphaFold monomer V2.0 prediction for glutamate dehydrogenase (P96110) · a predicted model of the same protein · chain C against A, TM-score 0.98
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 P96110
- Elsewhere: RCSB PDB 2TMG · PDBe 2TMG · UniProt P96110
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