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NN2101 antibody Fab fragment

Analyse NN2101 antibody Fab fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LUN
Type: protein
Length: 828 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NN2101
Pockets: 11 · best druggability 0.60

Structure

x-ray diffraction · 4 distinct chains · 8% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NN2101	protein	185	8% helix, 50% strand	—
B	NN2101	protein	217	6% helix, 51% strand	—
C	NN2101	protein	210	11% helix, 51% strand	—
D	NN2101	protein	216	6% helix, 52% strand	—

Pockets

11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	319	0.60	0.78	40	empty
2	60	0.56	0.89	22	empty
3	298	0.56	0.76	35	empty
4	221	0.54	0.78	41	empty
5	276	0.50	0.74	32	empty

Interfaces

4 interfaces between chains.

A–B · 1654 Å² buried · 13 hydrogen bonds · protein-protein
C–D · 1651 Å² buried · 15 hydrogen bonds · protein-protein
B–C · 119 Å² buried · 1 hydrogen bond · protein-protein
B–D · 116 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 7 disulfide (disulfide).

Compared structures

6LUN · NN2101 Antibody Fab fragment · 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 6LUN · PDBe 6LUN

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