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Catalytically non active S532A mutant of oligopeptidase B from S. proteomaculans with modified hinge region

Analyse Catalytically non active S532A mutant of oligopeptidase B from S.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7NE5
Type: protein
Length: 676 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oligopeptidase B
UniProt: B3VI58
Ligands: SPM
Pockets: 10 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Oligopeptidase B	protein	676	22% helix, 34% strand	B3VI58

Ligands and binding sites

SPM · Spermine · ligand · 2 copies · chains A

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

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	290	0.61	0.79	37	empty
2	300	0.58	0.78	34	empty
3	109	0.56	0.84	21	empty
4	187	0.51	0.78	34	empty
5	132	0.45	0.76	21	empty

Compared structures

7NE5 · catalytically non active S532A mutant of oligopeptidase B from S. proteomaculans with… · the same entry in another collection · 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 B3VI58
Elsewhere: RCSB PDB 7NE5 · PDBe 7NE5 · UniProt B3VI58

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