Research workbench

The structure of agmatinase from E. COLI at 1.8 a displaying urea and agmatine

Analyse The structure of agmatinase from E. COLI at 1.8 a displaying urea and agmatine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7LOL
Type: protein
Length: 294 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Agmatinase
EC: 3.5.3.11
UniProt: A0A4S5B4F2
Ligands: AG2, URE, MN
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Agmatinase (EC 3.5.3.11)	protein	294	41% helix, 15% strand	A0A4S5B4F2

Ligands and binding sites

AG2 · Agmatine · ligand · chains A
URE · Urea · ligand · chains A
MN · Manganese (II) ion · metal · 3 copies · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	60	0.28	0.74	17	AG2, URE

Compared structures

7LOL · The structure of Agmatinase from E. Coli at 1.8 A displaying urea and agmatine · 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 A0A4S5B4F2
Elsewhere: RCSB PDB 7LOL · PDBe 7LOL · UniProt A0A4S5B4F2

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