Research workbench

Crystal structure of an amidohydrolase (COG3618) from burkholderia multivorans (target efi-500235) with bound hepes, space group P3221

Analyse Crystal structure of an amidohydrolase (COG3618) from burkholderia multivorans… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DNM
Type: protein
Length: 287 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amidohydrolase 2
UniProt: A9ANE4
Ligands: ZN
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amidohydrolase 2	protein	287	51% helix, 14% strand	A9ANE4

Ligands and binding sites

ZN · Zinc ion · metal · chains A
GOL · Glycerol · additive · 3 copies · chains A
EPE · 4-(2-hydroxyethyl)-1-piperazine 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	232	0.59	0.80	31	EPE

Compared structures

4DNM · Crystal structure of an amidohydrolase (cog3618) from burkholderia multivorans (target… · 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 A9ANE4
Elsewhere: RCSB PDB 4DNM · PDBe 4DNM · UniProt A9ANE4

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