Research workbench
Structure of the trypanosome brucei factor H receptor bound to domain D5 of bovine factor H
Analyse Structure of the trypanosome brucei factor H receptor bound to domain D5 of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XZ6
- Type
- protein
- Length
- 544 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Garp domain-containing protein; Complement factor H
- UniProt
- Q57Z47, Q28085
- Pockets
- 3 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Garp domain-containing protein | protein | 213 | 86% helix, 0% strand | Q57Z47 |
| B, D | Complement factor H | protein | 59 | 0% helix, 44% strand | Q28085 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 279 | 0.51 | 0.75 | 35 | empty |
| 2 | 58 | 0.32 | 0.76 | 16 | empty |
| 3 | 63 | 0.31 | 0.75 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–B · 863 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 844 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 615 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 6XZ6 · Structure of the trypanosome brucei factor H receptor bound to domain D5 of bovine factor… · the same entry in another collection · chain A against A, TM-score 1.00
- Q28085 · AlphaFold monomer V2.0 prediction for complement factor H (Q28085) · a predicted model of the same protein · chain B against A, TM-score 0.89
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 Q57Z47
- Every structure of UniProt Q28085
- Elsewhere: RCSB PDB 6XZ6 · PDBe 6XZ6 · UniProt Q57Z47 · UniProt Q28085
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