MolNFT v1 · #154176 · protein

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

6K2H: “Structural characterization of mutated nrea protein in nitrate binding site from staphylococcus aureus.”. X-ray diffraction, 1 pocket (best druggability 0.55). MolNFT v1 #154176 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 6K2H
Type: protein
Length: 135 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nrea
UniProt: A0A0D1FZV0
Pockets: 1 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nrea	protein	135	35% helix, 27% strand	A0A0D1FZV0

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 3 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	168	0.55	0.80	21	empty

Compared structures

6K2H · 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 6K2H · PDBe 6K2H · UniProt A0A0D1FZV0

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