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Crystal structure of the C123S mutant of dienelactone hydrolase (dlh) bound with the pms moiety of the protease inhibitor, phenylmethylsulfonyl fluoride (pmsf)

Analyse Crystal structure of the C123S mutant of dienelactone hydrolase (dlh) bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1GGV
Type
protein
Length
232 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Dienelactone hydrolase
EC
3.1.1.45
UniProt
P0A114

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
ADienelactone hydrolase (EC 3.1.1.45)protein23242% helix, 21% strandP0A114

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

  • 1GGV · Crystal structure of the C123S mutant of dienelactone hydrolase (dlh) bound with the pms… · 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

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