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1ZIC

Crystal Structure Analysis of the dienelactone hydrolase (C123S, R206A) mutant- 1.7 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 Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 2719
ChainResidue
APRO75
AARG81
ASER203
ASER209
AHOH2722
AHOH2723
AHOH2798
AHOH2857
AHOH2878

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1101
ChainResidue
AGLU46
ATRP50
ATYR122
AALA205
AASN221
AHOH2800
AHOH2821

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1102
ChainResidue
AHIS172
ATYR212
AALA217
AALA218
AASN221
AHOH2811
AHOH2821

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 2024-08-21

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