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1ZIY

Crystal Structure Analysis of the dienelactone hydrolase mutant (C123S) bound with the PMS moiety of the protease inhibitor, Phenylmethylsulfonyl fluoride (PMSF)- 1.9 A

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 2719
ChainResidue
AARG81
ASEB123
AHIS202
ASER203
AARG206
ASER209
ASER210
AHOH2825

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 2720
ChainResidue
AALA72
AHOH2772
AMET1

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1101
ChainResidue
ATRP50
ATYR122
ATYR144
AALA205
AASN221
AGOL1102
AHOH2757
AHOH2808

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1102
ChainResidue
AHIS172
APHE173
ATYR212
AASN221
AGOL1101
AHOH2792
AHOH2813

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
ASEB123
AASP171
AHIS202

226707

PDB entries from 2024-10-30

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