MolNFT v1 · #185375 · protein

Crystal structure of beta-glucuronidase from acidobacterium capsulatum in complex with covalent inhibitor ME727

7PSI: “Crystal structure of beta-glucuronidase from acidobacterium capsulatum in complex with covalent inhibitor…”. X-ray diffraction, 2 ligands (8I4, SO4), 4 pockets (best druggability 0.61). MolNFT v1 #185375 on GenesisL1: 3D structure…

PDB: 7PSI
Type: protein
Length: 458 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-glucuronidase
UniProt: C1F2K5
Ligands: 8I4, SO4
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-glucuronidase	protein	458	30% helix, 29% strand	C1F2K5

Ligands and binding sites

8I4 · (2R,3S,5R,6R)-2,3,4,5,6-pentakis(oxidanyl)cyclohexane-1-carboxylic acid · ligand · chains A
SO4 · Sulfate ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	260	0.61	0.80	39	8I4
2	145	0.48	0.78	42	empty
3	90	0.42	0.79	19	empty
4	50	0.27	0.75	16	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

7PSI · Crystal structure of beta-glucuronidase from Acidobacterium capsulatum in complex with… · 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 C1F2K5
Elsewhere: RCSB PDB 7PSI · PDBe 7PSI · UniProt C1F2K5

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