Research workbench
Thermotoga maritima glutamate dehydrogenase mutant N97D, G376K
Analyse Thermotoga maritima glutamate dehydrogenase mutant N97D, G376K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1B3B
- Type
- protein
- Length
- 2,454 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
- 14 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Protein (glutamate dehydrogenase) (EC 1.4.1.3) | protein | 409 | 49% helix, 16% strand | P96110 |
Pockets
14 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1171 | 0.84 | 0.86 | 92 | empty |
| 2 | 1156 | 0.84 | 0.86 | 92 | empty |
| 3 | 1103 | 0.84 | 0.85 | 95 | empty |
| 4 | 1048 | 0.80 | 0.81 | 119 | empty |
| 5 | 1088 | 0.78 | 0.80 | 105 | empty |
Interfaces
12 interfaces between chains.
- A–F · 1031 Ų buried · 16 hydrogen bonds · protein-protein
- B–E · 1030 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 1018 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 895 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 879 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
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 1B3B · PDBe 1B3B · UniProt P96110
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