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1ZI9

Crystal Structure Analysis of the dienelactone hydrolase (E36D, C123S) mutant- 1.5 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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 2719
ChainResidue
APHE38
AARG81
ASER203
AARG206
ASER209
AGOL1101
AHOH2795

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 1101
ChainResidue
ATYR85
APHE173
AHIS202
AALA218
AGLU222
ASO42719
AHOH2737
AHOH2747
APHE38
AARG81

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1102
ChainResidue
AGLU46
ATRP50
ATYR122
ATYR144
AALA205
AASN221
AHOH2785
AHOH2841

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1103
ChainResidue
AHIS172
APHE173
ATYR212
AALA217
AALA218
AASN221
AHOH2737
AHOH2777
AHOH2785

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1104
ChainResidue
ATYR85
ALYS86
AGLN89
ATYR197
ASER215
AHOH2731
AHOH2739
AHOH2873
AHOH2886

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

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

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PDB entries from 2024-07-17

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