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1ZI8

Crystal Structure Analysis of the dienelactone hydrolase mutant(E36D, C123S, A134S, S208G, A229V, K234R)- 1.4 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0008806molecular_functioncarboxymethylenebutenolidase activity
A0016787molecular_functionhydrolase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 2719
ChainResidue
APHE38
AHOH2865
AHOH2869
APRO75
AARG81
ASER203
AARG206
ASER209
AGOL1101
AGOL1104
AHOH2774

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1101
ChainResidue
AASP36
AILE37
APHE38
AARG81
ASER123
AHIS202
ASO42719

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1102
ChainResidue
AGLU46
ATRP50
ATYR122
AALA205
AASN221
AHOH2755
AHOH2758

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1103
ChainResidue
AHIS172
APHE173
ATYR212
AALA217
AASN221
AHOH2755
AHOH2805

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1104
ChainResidue
AASP36
APHE38
ATYR122
ATYR145
ASER203
AARG206
ASO42719
AHOH2720
AHOH2760

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1105
ChainResidue
ATRP88
AGLN89
AALA214
ASER215
AHOH2759
AHOH2782
AHOH2815
AHOH2889

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
DetailsActive site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1din
ChainResidueDetails
ASER123
AASP171
AHIS202

246031

PDB entries from 2025-12-10

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