Research workbench

Structure of the catalytic domain of cwlv, N-acetylmuramoyl- L-alanine amidase from BACILLUS(PAENIBACILLUS) polymyxa VAR.COLISTINUS

Analyse Structure of the catalytic domain of cwlv, N-acetylmuramoyl- L-alanine amidase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JWQ
Type: protein
Length: 179 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-acetylmuramoyl-L-alanine amidase cwlv
EC: 3.5.1.28
UniProt: Q9LCR3
Ligands: ZN
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-acetylmuramoyl-L-alanine amidase cwlv (EC 3.5.1.28)	protein	179	42% helix, 24% strand	Q9LCR3

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	50	0.30	0.76	19	ZN

Compared structures

1JWQ · Structure of the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase 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 Q9LCR3
Elsewhere: RCSB PDB 1JWQ · PDBe 1JWQ · UniProt Q9LCR3

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