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Crystal structure of the bimagrumab Fab

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

PDB: 5NHW
Type: protein
Length: 426 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Anti-human actrii bimagrumab Fab heavy-chain; Anti-human actrii bimagrumab Fab light-chain
Pockets: 4 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H	Anti-human actrii bimagrumab Fab heavy-chain	protein	211	10% helix, 49% strand	—
L	Anti-human actrii bimagrumab Fab light-chain	protein	215	7% helix, 48% strand	—

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains H, L

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	657	0.64	0.74	79	GOL
2	110	0.39	0.75	23	empty
3	53	0.34	0.78	14	empty
4	55	0.26	0.73	18	empty

Interfaces

1 interface between chains.

H–L · 1712 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 1 modified (disulfide, cyclization).

Compared structures

5NHW · CRYSTAL STRUCTURE OF THE BIMAGRUMAB Fab · 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 5NHW · PDBe 5NHW

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