Research workbench
The complex structure of IPAH9.8-lrr and HGBP1
Analyse The complex structure of IPAH9.8-lrr and HGBP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LOJ
- Type
- protein
- Length
- 793 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Invasion plasmid antigen; Guanylate-binding protein 1
- EC
- 6.3.2.-, 3.6.5.-
- UniProt
- A0A380D7J9, P32455
- Ligands
- GDP
- Pockets
- 10 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Invasion plasmid antigen (EC 6.3.2.-) | protein | 222 | 19% helix, 12% strand | A0A380D7J9 |
| B | Guanylate-binding protein 1 (EC 3.6.5.-) | protein | 571 | 58% helix, 10% strand | P32455 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1049 | 0.76 | 0.79 | 78 | empty |
| 2 | 369 | 0.76 | 0.86 | 41 | empty |
| 3 | 227 | 0.76 | 0.89 | 38 | empty |
| 4 | 1066 | 0.74 | 0.77 | 92 | GDP |
| 5 | 640 | 0.69 | 0.77 | 68 | empty |
Interfaces
1 interface between chains.
- A–B · 684 Ų buried · 4 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 A0A380D7J9
- Every structure of UniProt P32455
- Elsewhere: RCSB PDB 6LOJ · PDBe 6LOJ · UniProt A0A380D7J9 · UniProt P32455
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