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Crystal structure of the Fab fragment of the human neutralizing anti- west nile virus mab CR4354

Analyse Crystal structure of the Fab fragment of the human neutralizing anti- west nile… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3N9G
Type: protein
Length: 450 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fab fragment of mab CR4354, heavy chain; Fab fragment of mab CR4354, light chain
Pockets: 5 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	Fab fragment of mab CR4354, heavy chain	protein	230	7% helix, 49% strand	—
L	Fab fragment of mab CR4354, light chain	protein	220	6% helix, 50% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	213	0.54	0.78	28	empty
2	145	0.47	0.77	24	empty
3	53	0.43	0.83	16	empty
4	99	0.41	0.77	19	empty
5	135	0.36	0.72	21	empty

Interfaces

1 interface between chains.

H–L · 1734 Å² buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide, 1 modified (disulfide, cyclization).

Compared structures

3N9G · Crystal structure of the Fab fragment of the human neutralizing anti-West Nile Virus MAb… · the same entry in another collection · chain L against L, 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 3N9G · PDBe 3N9G

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