Research workbench
Gltph mutant (S279E/D405N) in complex with aspartate and sodium ions
Analyse Gltph mutant (S279E/D405N) in complex with aspartate and sodium ions in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RCP
- Type
- protein
- Length
- 1,245 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate transporter homolog
- UniProt
- O59010
- Ligands
- ASP, NA
- Pockets
- 14 · best druggability 0.88
Structure
electron microscopy · 1 distinct chain · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Glutamate transporter homolog | protein | 415 | 81% helix, 0% strand | O59010 |
Ligands and binding sites
- ASP · Aspartic acid · ligand · 3 copies · chains A, B, C
- NA · Sodium ion · metal · 6 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 638 | 0.88 | 0.92 | 40 | empty |
| 2 | 288 | 0.52 | 0.73 | 32 | empty |
| 3 | 290 | 0.50 | 0.73 | 39 | empty |
| 4 | 267 | 0.50 | 0.73 | 36 | empty |
| 5 | 143 | 0.43 | 0.75 | 34 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1145 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 1144 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 1142 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 7RCP · GltPh mutant (S279E/D405N) in complex with aspartate and sodium ions · the same entry in another collection · chain A against A, TM-score 1.00
- O59010 · AlphaFold monomer V2.0 prediction for glutamate transporter homolog (O59010) · a predicted model of the same protein · chain C against A, TM-score 0.96
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 O59010
- Elsewhere: RCSB PDB 7RCP · PDBe 7RCP · UniProt O59010
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