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FAB C2E3

Analyse FAB C2E3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4R7N
Type: protein
Length: 4,292 residues
Chains: 20
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fab C2E3 heavy chain; Fab C2E3 light chain
Pockets: 20 · best druggability 0.80

Structure

x-ray diffraction · 3 distinct chains · 5% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E, G, I, K, M, O, Q, S	Fab C2E3 heavy chain	protein	218	6% helix, 48% strand	—
B, D, F, H, J, L, N, P, T	Fab C2E3 light chain	protein	211	5% helix, 47% strand	—
R	Fab C2E3 light chain	protein	213	5% helix, 46% strand	—

Pockets

20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	915	0.80	0.82	85	empty
2	949	0.75	0.78	104	empty
3	639	0.69	0.78	77	empty
4	610	0.68	0.77	75	empty
5	596	0.68	0.77	72	empty

Interfaces

37 interfaces between chains.

E–F · 1825 Å² buried · 15 hydrogen bonds · protein-protein
M–N · 1814 Å² buried · 15 hydrogen bonds · protein-protein
A–B · 1794 Å² buried · 15 hydrogen bonds · protein-protein
C–D · 1780 Å² buried · 17 hydrogen bonds · protein-protein
I–J · 1753 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 38 disulfide (disulfide).

Compared structures

4R7N · Fab C2E3 · 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
Elsewhere: RCSB PDB 4R7N · PDBe 4R7N

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