MolNFT v1 · #164890 · protein

Crystal structure of the omalizumab Fab SER81ARG and GLN83ARG light chain mutant

6TCQ: “Crystal structure of the omalizumab Fab SER81ARG and GLN83ARG light chain mutant”. X-ray diffraction, 3 pockets (best druggability 0.61). MolNFT v1 #164890 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6TCQ
Type: protein
Length: 434 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Omalizumab Fab SER81ARG and GLN83ARG light chain mutant
Pockets: 3 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	Omalizumab Fab SER81ARG and GLN83ARG light chain mutant	protein	217	7% helix, 53% strand	—
L	Omalizumab Fab SER81ARG and GLN83ARG light chain mutant	protein	217	6% helix, 53% strand	—

Ligands and binding sites

GOL · Glycerol · additive · chains H, L

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

Pockets

3 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	564	0.61	0.74	55	empty
2	52	0.53	0.89	19	GOL
3	88	0.35	0.75	22	empty

Interfaces

1 interface between chains.

H–L · 1850 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

6TCQ · Crystal structure of the omalizumab Fab Ser81Arg and Gln83Arg light chain mutant · the same entry in another collection · chain H against H, 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 6TCQ · PDBe 6TCQ

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.