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Solution structure of the plyg catalytic domain

Analyse Solution structure of the plyg catalytic domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2L47
Type: protein
Length: 165 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-acetylmuramoyl-L-alanine amidase
EC: 3.5.1.28
UniProt: Q8LTE6
Ligands: ZN
Pockets: 1 · best druggability 0.45

Structure

solution nmr · 1 distinct chain · 35% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28)	protein	165	35% helix, 16% strand	Q8LTE6

Ligands and binding sites

ZN · Zinc 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	131	0.45	0.77	21	empty

Compared structures

2L47 · Solution structure of the PlyG catalytic domain · 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 Q8LTE6
Elsewhere: RCSB PDB 2L47 · PDBe 2L47 · UniProt Q8LTE6

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