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Crystal structure of the isolated IGG4 CH3 domain
Analyse Crystal structure of the isolated IGG4 CH3 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4B53
- Type
- protein
- Length
- 206 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ig gamma-4 chain C region
- UniProt
- P01861
- Pockets
- 2 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ig gamma-4 chain C region | protein | 104 | 13% helix, 51% strand | P01861 |
| B | Ig gamma-4 chain C region | protein | 102 | 13% helix, 53% strand | P01861 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 5 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A, B
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
- ACT · Acetate ion · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.32 | 0.77 | 18 | empty |
| 2 | 65 | 0.28 | 0.73 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1067 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide, 2 modified (disulfide, cyclization).
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 P01861
- Elsewhere: RCSB PDB 4B53 · PDBe 4B53 · UniProt P01861
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