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Crystal structure of native human neuroserpin

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

PDB: 3FGQ
Type: protein
Length: 748 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neuroserpin
UniProt: Q99574
Pockets: 6 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Neuroserpin	protein	374	31% helix, 32% strand	Q99574

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	142	0.55	0.82	22	GOL
2	243	0.51	0.76	31	empty
3	52	0.51	0.87	16	empty
4	161	0.42	0.74	29	empty
5	122	0.40	0.75	21	empty

Interfaces

1 interface between chains.

A–B · 757 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

3FGQ · Crystal structure of native human neuroserpin · the same entry in another collection · chain A against A, TM-score 1.00
Q99574 · AlphaFold monomer V2.0 prediction for neuroserpin (Q99574) · a predicted model of the same protein · 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
Every structure of UniProt Q99574
Elsewhere: RCSB PDB 3FGQ · PDBe 3FGQ · UniProt Q99574

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