Research workbench

26-10 FAB:DIGOXIN complex-affinity and specificity due to surface complementarity

Analyse 26-10 FAB:DIGOXIN complex-affinity and specificity due to surface… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IGI
Type: protein
Length: 435 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: IGG2A-kappa 26-10 Fab (light chain); IGG2A-kappa 26-10 Fab (heavy chain)
Pockets: 6 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
L	IGG2A-kappa 26-10 Fab (light chain)	protein	218	6% helix, 53% strand	—
H	IGG2A-kappa 26-10 Fab (heavy chain)	protein	217	9% helix, 52% strand	—

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	143	0.51	0.79	23	empty
2	68	0.40	0.79	13	empty
3	83	0.33	0.74	20	empty
4	71	0.29	0.72	11	empty
5	75	0.29	0.73	19	empty

Interfaces

1 interface between chains.

L–H · 1964 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1IGI · 26-10 FAB:DIGOXIN complex-affinity and specificity due to surface complementarity · 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 1IGI · PDBe 1IGI

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