MolNFT v1 · #119177 · protein
Crystal structure of human complement C3B at 2.8 ångström resolution
5FO7 · Complement C3 beta chain: “Crystal structure of human complement C3B at 2.8 ångström resolution”. X-ray diffraction, 1 ligand (NAG), 19 pockets (best druggability 0.77). MolNFT v1 #119177 on GenesisL1: 3D structure, binding sites…
- PDB
- 5FO7
- Type
- protein
- Length
- 1,537 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Complement C3 beta chain; Complement C3B alpha' chain
- UniProt
- P01024
- Ligands
- NAG
- Pockets
- 19 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement C3 beta chain | protein | 637 | 7% helix, 52% strand | P01024 |
| B | Complement C3B alpha' chain | protein | 900 | 26% helix, 32% strand | P01024 |
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
19 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1065 | 0.77 | 0.79 | 85 | empty |
| 2 | 466 | 0.74 | 0.83 | 44 | empty |
| 3 | 363 | 0.67 | 0.81 | 55 | empty |
| 4 | 403 | 0.63 | 0.78 | 49 | empty |
| 5 | 213 | 0.62 | 0.82 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 5211 Ų buried · 67 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
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
- Elsewhere: RCSB PDB 5FO7 · PDBe 5FO7 · UniProt P01024
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