Research workbench
Structure of a complex between neisseria meningitidis factor H binding protein and ccps 6-7 of human complement factor H
Analyse Structure of a complex between neisseria meningitidis factor H binding protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2W81
- Type
- protein
- Length
- 1,083 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 · 6 distinct chains · 6% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement factor H | protein | 115 | 6% helix, 36% strand | P08603 |
| B | Complement factor H | protein | 121 | 8% helix, 36% strand | P08603 |
| C | Factor H binding protein | protein | 242 | 6% helix, 61% strand | Q9JXV4 |
| D | Factor H binding protein | protein | 243 | 4% helix, 58% strand | Q9JXV4 |
| E | Complement factor H | protein | 122 | 8% helix, 36% strand | P08603 |
| F | Factor H binding protein | protein | 240 | 6% helix, 60% strand | Q9JXV4 |
Pockets
13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1144 | 0.81 | 0.82 | 107 | empty |
| 2 | 1195 | 0.79 | 0.81 | 103 | empty |
| 3 | 880 | 0.77 | 0.80 | 77 | empty |
| 4 | 90 | 0.63 | 0.90 | 25 | empty |
| 5 | 197 | 0.55 | 0.79 | 37 | empty |
Interfaces
12 interfaces between chains.
- A–D · 1504 Ų buried · 23 hydrogen bonds · protein-protein
- E–F · 1430 Ų buried · 22 hydrogen bonds · protein-protein
- B–C · 1404 Ų buried · 20 hydrogen bonds · protein-protein
- D–F · 296 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 285 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 2W81 · Structure of a complex between Neisseria meningitidis factor H binding protein and CCPs… · 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 0.69
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 2W81 · PDBe 2W81 · UniProt P08603 · UniProt Q9JXV4
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