Research workbench

In a staphylococcal nuclease mutant the side-chain of a lysine replacing valine 66 is fully buried in the hydrophobic core

Analyse In a staphylococcal nuclease mutant the side-chain of a lysine replacing valine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2SNM
Type: protein
Length: 135 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Staphylococcal nuclease
EC: 3.1.31.1
UniProt: P00644
Ligands: THP, CA
Pockets: 1 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Staphylococcal nuclease (EC 3.1.31.1)	protein	135	27% helix, 30% strand	P00644

Ligands and binding sites

THP · Thymidine-3',5'-diphosphate · ligand · chains A
CA · Calcium ion · metal · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	137	0.46	0.77	29	CA, THP

Compared structures

2SNM · IN A STAPHYLOCOCCAL NUCLEASE MUTANT THE SIDE-CHAIN of A LYSINE REPLACING VALINE 66 IS… · 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 P00644
Elsewhere: RCSB PDB 2SNM · PDBe 2SNM · UniProt P00644

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