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Crystal structure of broadly neutralizing antibody HEPC74

Analyse Crystal structure of broadly neutralizing antibody HEPC74 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MEE
Type: protein
Length: 873 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Antibody HEPC74 heavy chain; Antibody HEPC74 light chain
Pockets: 7 · best druggability 0.81

Structure

x-ray diffraction · 3 distinct chains · 7% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Antibody HEPC74 heavy chain	protein	218	8% helix, 55% strand	—
B, D	Antibody HEPC74 light chain	protein	213	6% helix, 52% strand	—
C	Antibody HEPC74 heavy chain	protein	229	8% helix, 52% strand	—

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1095	0.81	0.82	155	empty
2	387	0.60	0.76	39	empty
3	248	0.58	0.79	31	empty
4	197	0.48	0.75	32	empty
5	54	0.35	0.79	17	empty

Interfaces

3 interfaces between chains.

C–D · 1976 Å² buried · 17 hydrogen bonds · protein-protein
A–B · 1932 Å² buried · 17 hydrogen bonds · protein-protein
B–D · 1126 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

6MEE · Crystal structure of broadly neutralizing antibody HEPC74 · the same entry in another collection · chain A against A, 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 6MEE · PDBe 6MEE

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