Research workbench
Structure of a complex between ccps 6 and 7 of human complement factor H and neisseria meningitidis fhbp variant 1 E283AE304A 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
- 4AYE
- Type
- protein
- Length
- 1,091 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
- 13 · best druggability 0.81
Structure
x-ray diffraction · 4 distinct chains · 6% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement factor H | protein | 123 | 6% helix, 37% strand | P08603 |
| B, E | Complement factor H | protein | 120 | 6% helix, 37% strand | P08603 |
| C, D | Factor H binding protein | protein | 243 | 6% helix, 60% strand | Q9JXV4 |
| F | Factor H binding protein | protein | 242 | 6% helix, 60% strand | Q9JXV4 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 19 copies · chains A, D, B, E, C, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1082 | 0.81 | 0.82 | 102 | EDO |
| 2 | 1061 | 0.79 | 0.80 | 86 | EDO |
| 3 | 715 | 0.74 | 0.80 | 74 | EDO |
| 4 | 71 | 0.51 | 0.85 | 26 | empty |
| 5 | 163 | 0.47 | 0.77 | 29 | empty |
Interfaces
12 interfaces between chains.
- A–D · 1614 Ų buried · 30 hydrogen bonds · protein-protein
- E–F · 1531 Ų buried · 29 hydrogen bonds · protein-protein
- B–C · 1437 Ų buried · 24 hydrogen bonds · protein-protein
- D–F · 269 Ų buried · 4 hydrogen bonds · protein-protein
- B–E · 253 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 4AYE · 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 0.72
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 4AYE · PDBe 4AYE · UniProt P08603 · UniProt Q9JXV4
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