MolNFT v1 · #172868 · protein

Crystal structure of the apo form of the N-acetylmuramyl-L-alanine amidase, AMI1, from mycobacterium abscessus.

7AGL · N-acetylmuramoyl-L-alanine amidase: “Crystal structure of the apo form of the N-acetylmuramyl-L-alanine amidase, AMI1, from mycobacterium…”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.57). MolNFT v1 #172868 on…

PDB: 7AGL
Type: protein
Length: 212 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-acetylmuramoyl-L-alanine amidase
UniProt: A0A418LHZ8
Ligands: ZN
Pockets: 1 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-acetylmuramoyl-L-alanine amidase	protein	212	37% helix, 22% strand	A0A418LHZ8

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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	164	0.57	0.82	30	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

7AGL · crystal structure of the apo form of the N-acetylmuramyl-L-alanine amidase, Ami1, 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 A0A418LHZ8
Elsewhere: RCSB PDB 7AGL · PDBe 7AGL · UniProt A0A418LHZ8

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