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Extending the half-life of a Fab fragment through generation of a humanised anti-human serum albumin (hsa) fv domain: an investigation into the correlation between affinity and serum half-life

Analyse Extending the half-life of a Fab fragment through generation of a humanised… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FUZ
Type: protein
Length: 438 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 645 Fab, heavy chain; 645 Fab, light chain
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	645 Fab, heavy chain	protein	222	5% helix, 50% strand	—
L	645 Fab, light chain	protein	216	6% helix, 51% strand	—

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	556	0.60	0.74	58	empty
2	273	0.52	0.75	39	empty

Interfaces

1 interface between chains.

H–L · 1808 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

5FUZ · Extending the half-life of a Fab fragment through generation of a humanised anti-Human… · 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
Elsewhere: RCSB PDB 5FUZ · PDBe 5FUZ

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