MolNFT v1 · #29772 · protein

Crystal structure analysis of the dienelactone hydrolase mutant (E36D, R105H, C123S, G211D, K234N)- 1.8 a

1ZIX · Carboxymethylenebutenolidase: “Crystal structure analysis of the dienelactone hydrolase mutant (E36D, R105H, C123S, G211D, K234N)- 1.8 a”. X-ray diffraction, 1 pocket (best druggability 0.43). MolNFT v1 #29772 on GenesisL1: 3D…

PDB: 1ZIX
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: P0A114
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carboxymethylenebutenolidase (EC 3.1.1.45)	protein	233	42% helix, 21% strand	P0A114

Ligands and binding sites

GOL · Glycerol · additive · 3 copies · 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	62	0.43	0.81	17	GOL

Compared structures

1ZIX · Crystal Structure Analysis of the dienelactone hydrolase mutant (E36D, R105H, C123S… · the same entry in another collection · chain A against A, TM-score 1.00
P0A114 · AlphaFold monomer V2.0 prediction for carboxymethylenebutenolidase (P0A114) · 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 P0A114
Elsewhere: RCSB PDB 1ZIX · PDBe 1ZIX · UniProt P0A114

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