Research workbench

CAT192 Fab insertion mutant H2/L2

Analyse CAT192 Fab insertion mutant H2/L2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AO0
Type: protein
Length: 427 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CAT192 Fab light chain; CAT192 Fab heavy chain
Ligands: SO4
Pockets: 4 · best druggability 0.50

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
L	CAT192 Fab light chain	protein	213	6% helix, 50% strand	—
H	CAT192 Fab heavy chain	protein	214	7% helix, 46% strand	—

Ligands and binding sites

SO4 · Sulfate ion · ion · 5 copies · chains H

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

Pockets

4 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	99	0.50	0.82	22	empty
2	152	0.45	0.76	19	empty
3	60	0.44	0.83	23	empty
4	50	0.30	0.76	15	empty

Interfaces

1 interface between chains.

L–H · 1276 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

6AO0 · CAT192 Fab Insertion Mutant H2/L2 · the same entry in another collection · chain L against L, 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 6AO0 · PDBe 6AO0

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