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The crystal structure of apo prostasin at 1.7 ångströms resolution

Analyse The crystal structure of apo prostasin at 1.7 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3E1X
Type: protein
Length: 247 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prostasin
EC: 3.4.21.-
UniProt: Q16651
Pockets: 3 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Prostasin (EC 3.4.21.-)	protein	247	11% helix, 34% strand	Q16651

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains B

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	97	0.37	0.75	17	empty
2	55	0.30	0.76	17	empty
3	60	0.29	0.74	20	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3E1X · The Crystal Structure of Apo Prostasin at 1.7 Angstroms Resolution · the same entry in another collection · chain B against B, TM-score 1.00
Q16651 · AlphaFold monomer V2.0 prediction for prostasin (Q16651) · a predicted model of the same protein · chain B against A, TM-score 0.96

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 Q16651
Elsewhere: RCSB PDB 3E1X · PDBe 3E1X · UniProt Q16651

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