MolNFT v1 · #117916 · protein

N-acetylmuramoyl-L-alanine amidase AMIC2 of nostoc punctiforme

5EMI · Cell wall HYDROLASE/AUTOLYSIN: “N-acetylmuramoyl-L-alanine amidase AMIC2 of nostoc punctiforme”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.30). MolNFT v1 #117916 on GenesisL1: 3D structure, binding sites and…

PDB: 5EMI
Type: protein
Length: 180 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell wall HYDROLASE/AUTOLYSIN
EC: 3.5.1.28
UniProt: B2J2S4
Ligands: ZN
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell wall HYDROLASE/AUTOLYSIN (EC 3.5.1.28)	protein	180	41% helix, 23% strand	B2J2S4

Ligands and binding sites

ZN · Zinc ion · metal · chains A
MRD · (4R)-2-methylpentane-2,4-diol · additive · 2 copies · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 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	54	0.30	0.76	18	ZN, MES

Compared structures

5EMI · N-acetylmuramoyl-L-alanine amidase AmiC2 of Nostoc punctiforme · 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 B2J2S4
Elsewhere: RCSB PDB 5EMI · PDBe 5EMI · UniProt B2J2S4

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