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4P92

Crystal structure of dienelactone hydrolase C123S mutant at 1.65 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0008806molecular_functioncarboxymethylenebutenolidase activity
A0009056biological_processcatabolic process
A0016787molecular_functionhydrolase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue SO4 A 301
ChainResidue
AARG45
ASER49
APRO175
AALA176
AHOH425
AHOH432
AHOH470
AHOH594

site_idAC2
Number of Residues10
Detailsbinding site for residue SO4 A 302
ChainResidue
ASER203
AARG206
ASER209
AHOH416
AHOH449
AHOH520
AHOH522
AHOH528
AHOH592
AARG81

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 303
ChainResidue
AMET1
AALA72
AHOH530

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. DleaairyarHqpYSNGKVGLvGYSlGGA
ChainResidueDetails
AASP99-ALA127

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE:
ChainResidueDetails
ASER123
AASP171
AHIS202

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PDB entries from 2024-10-02

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