MolNFT v1 · #181433 · protein

IGG2 Fc charge pair mutation version 1 (CPMV1)

7LUS · Immunoglobulin heavy constant gamma 2: “IGG2 Fc charge pair mutation version 1 (CPMV1)”. X-ray diffraction, 4 ligands (NAG, MAN, BMA), 2 pockets (best druggability 0.35). MolNFT v1 #181433 on GenesisL1: 3D structure, binding sites…

PDB: 7LUS
Type: protein
Length: 415 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Immunoglobulin heavy constant gamma 2
UniProt: P01859
Ligands: NAG, MAN, BMA, FUC
Pockets: 2 · best druggability 0.35

Structure

x-ray diffraction · 2 distinct chains · 11% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Immunoglobulin heavy constant gamma 2	protein	207	12% helix, 49% strand	P01859
A	Immunoglobulin heavy constant gamma 2	protein	208	11% helix, 50% strand	P01859

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains B, A
MAN · alpha-D-mannopyranose · sugar · 4 copies · chains B, A
BMA · beta-D-mannopyranose · sugar · 2 copies · chains B, A
FUC · alpha-L-fucopyranose · sugar · 2 copies · chains B, A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 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	63	0.35	0.78	15	empty
2	72	0.29	0.73	15	empty

Interfaces

1 interface between chains.

B–A · 1184 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

7LUS · IgG2 Fc Charge Pair Mutation version 1 (CPMv1) · the same entry in another collection · chain B against B, TM-score 1.00
P01859 · AlphaFold monomer V2.0 prediction for immunoglobulin heavy constant gamma 2 (P01859) · a predicted model of the same protein · chain B against A, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P01859
Elsewhere: RCSB PDB 7LUS · PDBe 7LUS · UniProt P01859

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