Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1ZI6

Crystal Structure Analysis of the dienelactone hydrolase (C123S) 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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 2719
ChainResidue
AARG45
ASER49
APRO175
AALA176
AHOH2753
AHOH2776
AHOH2796

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 2720
ChainResidue
AARG206
ASER209
AHOH2771
AHOH2849
AHOH2862
AARG81
ASER203

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2721
ChainResidue
AMET1
AALA72
AHOH2880
AHOH2903

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 1101
ChainResidue
ALYS86
AGLN89
ATYR197
AVAL213
ASER215
AALA216
AHOH2773
AHOH2787
AHOH2807
AHOH2840

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

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon