MolNFT v1 · #68711 · protein

Crystal structure of selenomethionine substituted E. COLI beta- glucuronidase

3K4A · Beta-glucuronidase: “Crystal structure of selenomethionine substituted E. COLI beta- glucuronidase”. X-ray diffraction, 18 pockets (best druggability 0.87). MolNFT v1 #68711 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 3K4A
Type: protein
Length: 1,194 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-glucuronidase
EC: 3.2.1.31
UniProt: P05804
Pockets: 18 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Beta-glucuronidase (EC 3.2.1.31)	protein	597	18% helix, 27% strand	P05804

Pockets

18 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1123	0.87	0.88	126	empty
2	85	0.70	0.94	17	empty
3	51	0.69	0.97	16	empty
4	356	0.67	0.81	45	empty
5	70	0.66	0.93	24	empty

Interfaces

1 interface between chains.

A–B · 1638 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 26 modified (engineered).

Compared structures

3K4A · Crystal structure of selenomethionine substituted E. coli beta-glucuronidase · the same entry in another collection · chain A against A, TM-score 1.00
P05804 · AlphaFold monomer V2.0 prediction for beta-glucuronidase (P05804) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P05804
Elsewhere: RCSB PDB 3K4A · PDBe 3K4A · UniProt P05804

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