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1ZIX

Crystal Structure Analysis of the dienelactone hydrolase mutant (E36D, R105H, C123S, G211D, K234N)- 1.8 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 GOL A 1101
ChainResidue
ATRP88
AGLN89
AALA214
ASER215
AHOH1128
AHOH1133
AHOH1226
AHOH1246

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1102
ChainResidue
APHE173
ATYR212
AALA217
AASN221
AHOH1121
AHOH1243
AHIS172

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1103
ChainResidue
AARG81
ASER203
AARG206
ASER209
ASER210

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. DleaaihyarHqpYSNGKVGLvGYSlGGA
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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