Research workbench
Idiotope-anti-idiotope Fab-Fab complex; D1.3-E225
Analyse Idiotope-anti-idiotope Fab-Fab complex; D1.3-E225 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CIC
- Type
- protein
- Length
- 863 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (ig heavy chain V regions)
- UniProt
- Q9R1A5, P01867, P01869
- Pockets
- 12 · best druggability 0.61
Structure
x-ray diffraction · 4 distinct chains · 6% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (ig heavy chain V regions) | protein | 214 | 6% helix, 48% strand | Q9R1A5 |
| B | Protein (ig heavy chain V regions) | protein | 217 | 7% helix, 53% strand | P01867 |
| C | Protein (ig heavy chain V regions) | protein | 214 | 7% helix, 53% strand | Q9R1A5 |
| D | Protein (ig heavy chain V regions) | protein | 218 | 6% helix, 51% strand | P01869 |
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 315 | 0.61 | 0.78 | 42 | empty |
| 2 | 501 | 0.60 | 0.75 | 43 | empty |
| 3 | 331 | 0.52 | 0.73 | 50 | empty |
| 4 | 82 | 0.46 | 0.81 | 22 | empty |
| 5 | 161 | 0.45 | 0.76 | 23 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1940 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 1862 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 432 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 318 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 252 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 1CIC · Idiotope-anti-idiotope Fab-Fab complex; D1.3-E225 · the same entry in another collection · chain B against B, TM-score 1.00
- P01869 · AlphaFold monomer V2.0 prediction for ig gamma-1 chain C region, membrane-bound form… · a predicted model of the same protein · chain D against A, TM-score 0.53
- P01867 · AlphaFold monomer V2.0 prediction for ig gamma-2B chain C region (P01867) · a predicted model of the same protein · chain B 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 Q9R1A5
- Every structure of UniProt P01867
- Every structure of UniProt P01869
- Elsewhere: RCSB PDB 1CIC · PDBe 1CIC · UniProt Q9R1A5 · UniProt P01867 · UniProt P01869
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