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Structure of dienelactone hydrolase at 1.85 a resolution crystallised in the C2 space group

Analyse Structure of dienelactone hydrolase at 1.85 a resolution crystallised in the C2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4P93
Type: protein
Length: 466 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carboxymethylenebutenolidase
EC: 3.1.1.45
UniProt: P0A115
Pockets: 4 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Carboxymethylenebutenolidase (EC 3.1.1.45)	protein	233	39% helix, 21% strand	P0A115

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	564	0.67	0.77	57	empty
2	225	0.53	0.77	29	empty
3	83	0.37	0.76	18	empty
4	57	0.32	0.77	18	empty

Interfaces

1 interface between chains.

A–B · 484 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

4P93 · Structure of Dienelactone Hydrolase at 1.85 A resolution crystallised in the C2 space… · 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 0.99

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 4P93 · PDBe 4P93 · UniProt P0A115

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