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Crystal structure of human Fab CAP256-VRC26.01, a potent V1V2-directed HIV-1 neutralizing antibody

Analyse Crystal structure of human Fab CAP256-VRC26.01, a potent V1V2-directed HIV-1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4OCR
Type: protein
Length: 449 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CAP256-VRC26.01 light chain; CAP256-VRC26.01 heavy chain
Pockets: 4 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
L	CAP256-VRC26.01 light chain	protein	216	9% helix, 49% strand	—
H	CAP256-VRC26.01 heavy chain	protein	233	8% helix, 48% strand	—

Pockets

4 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	800	0.70	0.76	75	empty
2	173	0.50	0.78	37	empty
3	125	0.43	0.76	24	empty
4	60	0.27	0.73	16	empty

Interfaces

1 interface between chains.

L–H · 1933 Å² buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

4OCR · Crystal structure of human Fab CAP256-VRC26.01, a potent V1V2-directed HIV-1 neutralizing… · 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 4OCR · PDBe 4OCR

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