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X-ray analyses of aspartic proteases. II. three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 ångströms resolution

Analyse X-ray analyses of aspartic proteases. II. three-dimensional structure of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5PEP
Type: protein
Length: 326 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.34
Source: Sus scrofa
Molecule: Pepsin
EC: 3.4.23.1
UniProt: P00791
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · resolution 2.34 · 1 distinct chain · 13% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pepsin (EC 3.4.23.1)	protein	326	13% helix, 45% strand	P00791

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	315	0.63	0.79	39	empty
2	54	0.28	0.75	16	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

5PEP · X-ray analyses of aspartic proteases. II. three-dimensional structure of the hexagonal… · the same entry in another collection · chain A against A, TM-score 1.00
P00791 · AlphaFold monomer V2.0 prediction for pepsin a (P00791) · a predicted model of the same protein · chain A 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 P00791
Elsewhere: RCSB PDB 5PEP · PDBe 5PEP · UniProt P00791

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