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Crystal structure analysis of an amidase from nesterenkonia sp.

Analyse Crystal structure analysis of an amidase from nesterenkonia sp. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HKX
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amidase
EC: 3.5.1.4
UniProt: D0VWZ1
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amidase (EC 3.5.1.4)	protein	263	34% helix, 28% strand	D0VWZ1

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	84	0.40	0.77	20	empty

Compared structures

3HKX · Crystal structure analysis of an amidase from Nesterenkonia sp. · 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 3HKX · PDBe 3HKX · UniProt D0VWZ1

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