Research workbench
Crystal structure of APE1551, an anti-human ngf Fab with a nine amino acid insertion in cdr H1
Analyse Crystal structure of APE1551, an anti-human ngf Fab with a nine amino acid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NWU
- Type
- protein
- Length
- 451 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- APE1551 ab Fab heavy chain; APE1551 ab Fab light chain
- UniProt
- P01857, Q8TCD0
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | APE1551 ab Fab heavy chain | protein | 231 | 9% helix, 53% strand | P01857 |
| L | APE1551 ab Fab light chain | protein | 220 | 5% helix, 52% strand | Q8TCD0 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 589 | 0.63 | 0.75 | 58 | empty |
| 2 | 201 | 0.52 | 0.77 | 30 | empty |
| 3 | 62 | 0.30 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- H–L · 2126 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 4NWU · Crystal structure of APE1551, an anti-human NGF Fab with a nine amino acid insertion in… · the same entry in another collection · chain H against H, 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
- Every structure of UniProt P01857
- Every structure of UniProt Q8TCD0
- Elsewhere: RCSB PDB 4NWU · PDBe 4NWU · UniProt P01857 · UniProt Q8TCD0
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