Research workbench

Crystal structure of FM329, a recombinant Fab adopted from cetuximab

Analyse Crystal structure of FM329, a recombinant Fab adopted from cetuximab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5GZ0
Type: protein
Length: 868 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FM329 light chain; FM329 heavy chain
Pockets: 7 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	FM329 light chain	protein	213	5% helix, 52% strand	—
B, D	FM329 heavy chain	protein	221	8% helix, 51% strand	—

Pockets

7 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	902	0.75	0.79	118	empty
2	609	0.64	0.75	58	empty
3	220	0.49	0.75	30	empty
4	122	0.42	0.76	29	empty
5	72	0.35	0.77	15	empty

Interfaces

3 interfaces between chains.

C–D · 1853 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 1845 Å² buried · 18 hydrogen bonds · protein-protein
A–C · 662 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

5GZ0 · Crystal structure of FM329, a recombinant Fab adopted from cetuximab · 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 5GZ0 · PDBe 5GZ0

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