MolNFT v1 · #101421 · protein

Knob-into-hole IgG Fc

4NQS · Ig gamma-1 chain C region: “Knob-into-hole IgG Fc”. X-ray diffraction, 6 pockets (best druggability 0.80). MolNFT v1 #101421 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4NQS
Type: protein
Length: 968 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ig gamma-1 chain C region; Miniz
UniProt: P01857
Pockets: 6 · best druggability 0.80

Structure

x-ray diffraction · 4 distinct chains · 14% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ig gamma-1 chain C region	protein	210	10% helix, 49% strand	P01857
B, H	Ig gamma-1 chain C region	protein	207	11% helix, 49% strand	P01857
D, E, I, J	Miniz	protein	34	76% helix, 0% strand	—
G	Ig gamma-1 chain C region	protein	208	10% helix, 49% strand	P01857

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	955	0.80	0.82	74	empty
2	105	0.35	0.74	18	empty
3	57	0.32	0.76	20	empty
4	68	0.31	0.75	18	empty
5	57	0.26	0.73	13	empty

Interfaces

12 interfaces between chains.

A–B · 1244 Å² buried · 14 hydrogen bonds · protein-protein
G–H · 1206 Å² buried · 15 hydrogen bonds · protein-protein
B–E · 761 Å² buried · 6 hydrogen bonds · protein-protein
A–D · 742 Å² buried · 5 hydrogen bonds · protein-protein
H–J · 732 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

4NQS · Knob-into-hole IgG Fc · 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
Every structure of UniProt P01857
Elsewhere: RCSB PDB 4NQS · PDBe 4NQS · UniProt P01857

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