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Structure of prostasin at 1.3 ångströms resolution in complex with a calcium ion.

Analyse Structure of prostasin at 1.3 ångströms resolution in complex with a calcium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GYL
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
Ligands: CA
Pockets: 2 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Prostasin (EC 3.4.21.-)	protein	247	12% helix, 34% strand	Q16651

Ligands and binding sites

CA · Calcium ion · metal · chains B
GOL · Glycerol · additive · 2 copies · chains B

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

Pockets

2 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	219	0.57	0.79	40	CA
2	55	0.29	0.75	15	GOL

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3GYL · Structure of Prostasin at 1.3 Angstroms resolution in complex with a Calcium Ion. · 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 3GYL · PDBe 3GYL · UniProt Q16651

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