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Crystal structure of human Fab CAP256-VRC26.10, a potent V1V2-directed HIV-1 neutralizing antibody

Analyse Crystal structure of human Fab CAP256-VRC26.10, 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: 4OCS
Type: protein
Length: 442 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CAP256-VRC26.10 light chain; CAP256-VRC26.10 heavy chain
Pockets: 5 · best druggability 0.44

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
L	CAP256-VRC26.10 light chain	protein	212	6% helix, 50% strand	—
H	CAP256-VRC26.10 heavy chain	protein	230	8% helix, 49% strand	—

Pockets

5 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	81	0.44	0.81	21	empty
2	170	0.43	0.74	28	empty
3	111	0.38	0.74	25	empty
4	62	0.28	0.74	16	empty
5	51	0.26	0.73	12	empty

Interfaces

1 interface between chains.

L–H · 1735 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

4OCS · Crystal structure of human Fab CAP256-VRC26.10, a potent V1V2-directed HIV-1 neutralizing… · the same entry in another collection · chain L against L, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 4OCS · PDBe 4OCS

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