Research workbench
Four models of human factor H determined by solution scattering curve-fitting and homology modelling
Analyse Four models of human factor H determined by solution scattering curve-fitting… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HAQ
- Type
- protein
- Length
- 1,213 residues
- Chains
- 1
- Method
- solution scattering
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Complement factor H
- UniProt
- P08603
- Pockets
- 1 · best druggability 0.32
Structure
solution scattering · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement factor H | protein | 1213 | 0% helix, 0% strand | P08603 |
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 | 62 | 0.32 | 0.74 | 29 | empty |
Compared structures
- 1HAQ · Four models of human factor H determined by solution scattering curve-fitting and… · the same entry in another collection · chain A against A, TM-score 1.00
- P08603 · AlphaFold monomer V2.0 prediction for complement factor H (P08603) · a predicted model of the same protein · chain A against A, TM-score 0.11
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 P08603
- Elsewhere: RCSB PDB 1HAQ · PDBe 1HAQ · UniProt P08603
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