Research workbench

X-ray structures of fragments from binding and nonbinding versions of a humanized anti-CD18 antibody: structural indications of the key role of vh residues 59 to 65

Analyse X-ray structures of fragments from binding and nonbinding versions of a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FGW
Type: protein
Length: 434 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: H52 Fab (light chain); H52 Fab (heavy chain)
Pockets: 4 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
L	H52 Fab (light chain)	protein	214	6% helix, 48% strand	—
H	H52 Fab (heavy chain)	protein	220	8% helix, 51% strand	—

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	78	0.44	0.81	20	empty
2	190	0.44	0.73	31	empty
3	183	0.41	0.72	28	empty
4	57	0.29	0.75	17	empty

Interfaces

1 interface between chains.

L–H · 1847 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

2FGW · X-ray structures of fragments from binding and nonbinding versions of a humanized… · 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 2FGW · PDBe 2FGW

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.