MolNFT v1 · #37615 · protein

Crystal structure of anti-SARS M396 antibody

2G75 · IgG heavy chain: “Crystal structure of anti-SARS M396 antibody”. X-ray diffraction, 11 pockets (best druggability 0.56). MolNFT v1 #37615 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2G75
Type: protein
Length: 858 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: IgG heavy chain; IgG light chain
Pockets: 11 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	IgG heavy chain	protein	218	4% helix, 51% strand	—
B, D	IgG light chain	protein	211	6% helix, 50% strand	—

Pockets

11 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	403	0.56	0.74	47	empty
2	186	0.54	0.79	32	empty
3	96	0.48	0.81	23	empty
4	96	0.48	0.81	23	empty
5	127	0.47	0.78	18	empty

Interfaces

3 interfaces between chains.

A–B · 1719 Å² buried · 13 hydrogen bonds · protein-protein
C–D · 1710 Å² buried · 15 hydrogen bonds · protein-protein
A–C · 110 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

2G75 · Crystal Structure of anti-SARS m396 Antibody · 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 2G75 · PDBe 2G75

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