Research workbench

Q118A mutant of SO1698 protein, an aspartic peptidase from shewanella oneidensis

Analyse Q118A mutant of SO1698 protein, an aspartic peptidase from shewanella oneidensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NJN
Type: protein
Length: 243 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidase
UniProt: Q8EGA7
Ligands: CA

Structure

x-ray diffraction · 3 distinct chains · 0% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Peptidase	protein	114	0% helix, 55% strand	Q8EGA7
B	Peptidase	protein	8	0% helix, 50% strand	Q8EGA7
D	Peptidase	protein	7	0% helix, 57% strand	Q8EGA7

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A, C
MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A

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

Interfaces

3 interfaces between chains.

A–C · 1255 Å² buried · 26 hydrogen bonds · protein-protein
A–B · 672 Å² buried · 24 hydrogen bonds · protein-protein
C–D · 627 Å² buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 isopeptide (isopeptide).

Compared structures

3NJN · Q118A mutant of SO1698 protein, an aspartic peptidase from Shewanella oneidensis · 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 Q8EGA7
Elsewhere: RCSB PDB 3NJN · PDBe 3NJN · UniProt Q8EGA7

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.