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A C145A mutant of nesterenkonia AN1 amidase bound to propionamide

Analyse A C145A mutant of nesterenkonia AN1 amidase bound to propionamide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NYE
Type: protein
Length: 261 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amidase
EC: 3.5.1.4
UniProt: D0VWZ1
Ligands: ROP, CL
Pockets: 2 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amidase (EC 3.5.1.4)	protein	261	34% helix, 27% strand	D0VWZ1

Ligands and binding sites

ROP · Propionamide · ligand · 2 copies · chains A
CL · Chloride ion · ion · chains A
PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	68	0.40	0.80	21	ROP
2	52	0.25	0.73	10	empty

Compared structures

5NYE · A C145A mutant of Nesterenkonia AN1 amidase bound to propionamide · 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 D0VWZ1
Elsewhere: RCSB PDB 5NYE · PDBe 5NYE · UniProt D0VWZ1

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