MolNFT v1 · #84193 · protein
The structure of the two N-terminal domains of complement factor H related protein 1 shows formation of a novel dimerisation interface
3ZD2 · Complement factor H-related protein 1: “The structure of the two N-terminal domains of complement factor H related protein 1 shows formation of a…”. X-ray diffraction, 3 pockets (best druggability 0.71). MolNFT v1 #84193 on…
- PDB
- 3ZD2
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Complement factor H-related protein 1
- UniProt
- Q03591
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 1% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement factor H-related protein 1 | protein | 125 | 2% helix, 37% strand | Q03591 |
| B | Complement factor H-related protein 1 | protein | 119 | 0% helix, 39% strand | Q03591 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 16 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 197 | 0.71 | 0.88 | 27 | EDO |
| 2 | 159 | 0.49 | 0.77 | 27 | EDO |
| 3 | 159 | 0.44 | 0.75 | 30 | EDO |
Interfaces
1 interface between chains.
- A–B · 816 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 3ZD2 · The structure of the two N-terminal domains of complement factor H related protein 1… · the same entry in another collection · chain A against A, TM-score 1.00
- Q03591 · AlphaFold monomer V2.0 prediction for complement factor H-related protein 1 (Q03591) · a predicted model of the same protein · chain B 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 Q03591
- Elsewhere: RCSB PDB 3ZD2 · PDBe 3ZD2 · UniProt Q03591
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