MolNFT v1 · #171801 · protein
Crystal structure of complex between FH19-20 and fhba protein from borrelia hermsii
6ZH1 · Factor H-binding protein a: “Crystal structure of complex between FH19-20 and fhba protein from borrelia hermsii”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.61). MolNFT v1 #171801 on GenesisL1: 3D structure…
- PDB
- 6ZH1
- Type
- protein
- Length
- 285 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Factor H-binding protein a; Complement factor H
- UniProt
- W5SB08, P08603
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Factor H-binding protein a | protein | 159 | 76% helix, 0% strand | W5SB08 |
| B | Complement factor H | protein | 126 | 5% helix, 38% strand | P08603 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 250 | 0.61 | 0.80 | 29 | EDO |
| 2 | 204 | 0.55 | 0.79 | 30 | EDO |
Interfaces
1 interface between chains.
- A–B · 1184 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6ZH1 · Crystal structure of complex between FH19-20 and FhbA protein from Borrelia hermsii · 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 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 W5SB08
- Every structure of UniProt P08603
- Elsewhere: RCSB PDB 6ZH1 · PDBe 6ZH1 · UniProt W5SB08 · UniProt P08603
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