Research workbench
Structure of complement proteins complex
Analyse Structure of complement proteins complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5O35
- Type
- protein
- Length
- 1,921 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Complement C3; Complement factor H,COMPLEMENT factor H
- UniProt
- P01024, P08603
- Ligands
- NAG
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 15% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement C3 | protein | 642 | 7% helix, 52% strand | P01024 |
| B | Complement C3 | protein | 912 | 26% helix, 32% strand | P01024 |
| C | Complement factor H,COMPLEMENT factor H | protein | 367 | 2% helix, 38% strand | P08603 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 923 | 0.81 | 0.83 | 87 | empty |
| 2 | 751 | 0.75 | 0.80 | 67 | empty |
| 3 | 776 | 0.71 | 0.77 | 55 | empty |
| 4 | 382 | 0.69 | 0.82 | 41 | empty |
| 5 | 532 | 0.68 | 0.78 | 67 | empty |
Interfaces
3 interfaces between chains.
- A–B · 5305 Ų buried · 64 hydrogen bonds · protein-protein
- B–C · 2226 Ų buried · 25 hydrogen bonds · protein-protein
- A–C · 891 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 21 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 5O35 · Structure of complement proteins complex · the same entry in another collection · chain A against A, TM-score 1.00
- P01024 · AlphaFold monomer V2.0 prediction for complement C3 (P01024) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P08603 · AlphaFold monomer V2.0 prediction for complement factor H (P08603) · a predicted model of the same protein · chain C against A, TM-score 0.50
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 P01024
- Every structure of UniProt P08603
- Elsewhere: RCSB PDB 5O35 · PDBe 5O35 · UniProt P01024 · UniProt P08603
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