Research workbench
Structure of a complex between ccps 6 and 7 of human complement factor H and neisseria meningitidis fhbp variant 1 R106A mutant
Analyse Structure of a complex between ccps 6 and 7 of human complement factor H and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AYD
- Type
- protein
- Length
- 1,084 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Complement factor H; Factor H binding protein
- UniProt
- P08603, Q9JXV4
- Pockets
- 11 · best druggability 0.82
Structure
x-ray diffraction · 6 distinct chains · 6% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement factor H | protein | 123 | 6% helix, 37% strand | P08603 |
| B | Complement factor H | protein | 117 | 6% helix, 38% strand | P08603 |
| C | Factor H binding protein | protein | 238 | 6% helix, 60% strand | Q9JXV4 |
| D | Factor H binding protein | protein | 243 | 6% helix, 62% strand | Q9JXV4 |
| E | Complement factor H | protein | 121 | 8% helix, 36% strand | P08603 |
| F | Factor H binding protein | protein | 242 | 6% helix, 62% strand | Q9JXV4 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 4 copies · chains B, C, A, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 642 | 0.82 | 0.87 | 87 | empty |
| 2 | 318 | 0.74 | 0.86 | 45 | empty |
| 3 | 340 | 0.73 | 0.85 | 35 | empty |
| 4 | 574 | 0.66 | 0.77 | 43 | empty |
| 5 | 115 | 0.59 | 0.85 | 28 | empty |
Interfaces
12 interfaces between chains.
- A–D · 1340 Ų buried · 28 hydrogen bonds · protein-protein
- E–F · 1204 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 1131 Ų buried · 20 hydrogen bonds · protein-protein
- D–F · 377 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 262 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 4AYD · Structure of a complex between CCPs 6 and 7 of Human Complement Factor H and Neisseria… · the same entry in another collection · chain F against F, TM-score 1.00
- P08603 · AlphaFold monomer V2.0 prediction for complement factor H (P08603) · a predicted model of the same protein · chain E against A, TM-score 0.73
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
- Every structure of UniProt Q9JXV4
- Elsewhere: RCSB PDB 4AYD · PDBe 4AYD · UniProt P08603 · UniProt Q9JXV4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.