Research workbench
Structure of an activity suppressing Fab fragment to cytochrome P450 aromatase
Analyse Structure of an activity suppressing Fab fragment to cytochrome P450 aromatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 32C2
- Type
- protein
- Length
- 435 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- IGG1 antibody 32C2
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | IGG1 antibody 32C2 | protein | 217 | 4% helix, 45% strand | — |
| B | IGG1 antibody 32C2 | protein | 218 | 7% helix, 47% strand | — |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 415 | 0.57 | 0.74 | 54 | empty |
| 2 | 77 | 0.57 | 0.87 | 21 | empty |
| 3 | 196 | 0.46 | 0.74 | 31 | empty |
| 4 | 50 | 0.36 | 0.80 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1844 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 32C2 · Structure of an activity suppressing Fab fragment to cytochrome P450 aromatase · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 32C2 · PDBe 32C2
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