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Crystal structure of dienelactone hydrolase (C123S) at 1.70 a resolution

Analyse Crystal structure of dienelactone hydrolase (C123S) at 1.70 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4U2B
Type: protein
Length: 233 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carboxymethylenebutenolidase
EC: 3.1.1.45
UniProt: P0A115
Ligands: SO4
Pockets: 2 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carboxymethylenebutenolidase (EC 3.1.1.45)	protein	233	41% helix, 21% strand	P0A115

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	59	0.41	0.81	17	empty
2	50	0.35	0.79	17	SO4

Compared structures

4U2B · Crystal structure of dienelactone hydrolase (C123S) at 1.70 A resolution · the same entry in another collection · chain A against A, TM-score 1.00
P0A115 · AlphaFold monomer V2.0 prediction for carboxymethylenebutenolidase (P0A115) · a predicted model of the same protein · 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 P0A115
Elsewhere: RCSB PDB 4U2B · PDBe 4U2B · UniProt P0A115

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