Research workbench
Crystal structure of a double loop deletion mutant in GC1QR/C1QBP/HABP-1
Analyse Crystal structure of a double loop deletion mutant in GC1QR/C1QBP/HABP-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TE3
- Type
- protein
- Length
- 165 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Complement component 1 Q subcomponent-binding protein, mitochondrial
- UniProt
- Q07021
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement component 1 Q subcomponent-binding protein, mitochondrial | protein | 165 | 38% helix, 28% strand | Q07021 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 114 | 0.36 | 0.74 | 21 | empty |
Compared structures
- 7TE3 · Crystal Structure of a Double Loop Deletion Mutant in gC1qR/C1qBP/HABP-1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q07021 · AlphaFold monomer V2.0 prediction for complement component 1 Q subcomponent-binding… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q07021
- Elsewhere: RCSB PDB 7TE3 · PDBe 7TE3 · UniProt Q07021
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