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1ZJ4

Crystal Structure Analysis of the dienelactone hydrolase mutant (E36D, C123S) bound with the PMS moiety of the protease inhibitor, Phenylmethylsulfonyl fluoride (PMSF)- 1.7 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0008806molecular_functioncarboxymethylenebutenolidase activity
A0016787molecular_functionhydrolase activity
A0019439biological_processobsolete aromatic compound catabolic process
A0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 2719
ChainResidue
AARG81
ASEB123
APHE173
ASER203
AARG206
ASER209
ASER210

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 2720
ChainResidue
AGLU150
ALYS151
ATYR212
AALA214
AHOH2730
AHOH2761
AHOH2765
AHOH2787
AVAL147
AGLY148

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1101
ChainResidue
ATRP88
AGLN89
AVAL213
AALA214
ASER215
AHOH2730
AHOH2765

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
ASEB123
AASP171
AHIS202

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PDB entries from 2024-06-12

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