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Crystal structure of human N12-I2 Fab, an adcc and neutralizing anti- HIV-1 env antibody

Analyse Crystal structure of human N12-I2 Fab, an adcc and neutralizing anti- HIV-1 env… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3QEG
Type: protein
Length: 429 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fab fragment of human anti-HIV antibody N12-I2, heavy chain; Fab fragment of human…
Pockets: 3 · best druggability 0.56

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	Fab fragment of human anti-HIV antibody N12-I2, heavy chain	protein	216	7% helix, 49% strand	—
L	Fab fragment of human anti-HIV antibody N12-I2, light chain	protein	213	7% helix, 53% strand	—

Pockets

3 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	377	0.56	0.74	54	empty
2	56	0.48	0.85	19	empty
3	88	0.33	0.74	18	empty

Interfaces

1 interface between chains.

H–L · 1786 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3QEG · Crystal structure of human N12-i2 Fab, an ADCC and neutralizing anti-HIV-1 Env antibody · 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 3QEG · PDBe 3QEG

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