Research workbench
Mouse gitr (mgitr) with dta-1 Fab fragment
Analyse Mouse gitr (mgitr) with dta-1 Fab fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RFP
- Type
- protein
- Length
- 1,114 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tumor necrosis factor receptor superfamily member 18, enhanced green fluorescent protein…
- UniProt
- O35714
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 3 distinct chains · 6% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Tumor necrosis factor receptor superfamily member 18, enhanced green fluorescent protein | protein | 118 | 3% helix, 23% strand | O35714 |
| H, I | Dta-1 (heavy chain) | protein | 218 | 7% helix, 44% strand | — |
| L, M | Dta-1 (light chain) | protein | 221 | 6% helix, 46% strand | — |
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1117 | 0.83 | 0.85 | 145 | empty |
| 2 | 617 | 0.78 | 0.84 | 93 | empty |
| 3 | 662 | 0.78 | 0.83 | 89 | empty |
| 4 | 738 | 0.77 | 0.82 | 82 | empty |
| 5 | 636 | 0.73 | 0.80 | 101 | empty |
Interfaces
8 interfaces between chains.
- I–M · 644 Ų buried · 0 hydrogen bonds · protein-protein
- H–L · 643 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 390 Ų buried · 0 hydrogen bonds · protein-protein
- B–M · 263 Ų buried · 0 hydrogen bonds · protein-protein
- A–L · 257 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 23 disulfide (disulfide).
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 O35714
- Elsewhere: RCSB PDB 7RFP · PDBe 7RFP · UniProt O35714
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