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Crystal structure of RV3717 reveals a novel amidase from M. tuberculosis

Analyse Crystal structure of RV3717 reveals a novel amidase from M. tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LQ6
Type: protein
Length: 213 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-acetymuramyl-L-alanine amidase-related protein
UniProt: O69684
Ligands: PT, ZN, CL, SO4
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-acetymuramyl-L-alanine amidase-related protein	protein	213	39% helix, 22% strand	O69684

Ligands and binding sites

PT · Platinum (II) ion · metal · 3 copies · chains A
ZN · Zinc ion · metal · chains A
CL · Chloride ion · ion · 4 copies · chains A
SO4 · Sulfate ion · ion · 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	198	0.63	0.84	36	ZN, CL, PT

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4LQ6 · Crystal structure of Rv3717 reveals a novel amidase from M. tuberculosis · 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 O69684
Elsewhere: RCSB PDB 4LQ6 · PDBe 4LQ6 · UniProt O69684

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