Research workbench

Structural characterization of mutated nrea protein in nitrate binding site from staphylococcus aureus

Analyse Structural characterization of mutated nrea protein in nitrate binding site… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IZK
Type: protein
Length: 284 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nrea
UniProt: A0A0D1FZV0
Ligands: CL
Pockets: 3 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Nrea	protein	142	37% helix, 28% strand	A0A0D1FZV0

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A, B
IMD · Imidazole · additive · 2 copies · chains A, B
TLA · L(+)-tartaric acid · additive · chains A, 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	66	0.54	0.87	16	TLA
2	105	0.44	0.78	16	empty
3	93	0.42	0.78	15	empty

Interfaces

1 interface between chains.

A–B · 1050 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

6IZK · Structural characterization of mutated NreA protein in nitrate binding site from… · 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 A0A0D1FZV0
Elsewhere: RCSB PDB 6IZK · PDBe 6IZK · UniProt A0A0D1FZV0

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