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1ZJ5

Crystal Structure Analysis of the dienelactone hydrolase mutant (E36D, C123S, A134S, S208G, A229V, K234R) 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
A0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 2719
ChainResidue
APHE38
AHOH2761
AHOH2762
APRO75
AARG81
ASEB123
APHE173
ASER203
AARG206
ASER209
AHOH2745

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 2720
ChainResidue
AGLY148
ATYR212
AALA214
AGOL1101
AHOH2726
AHOH2741
AHOH2751
AHOH2825

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1101
ChainResidue
AVAL147
AGLY148
AGLU150
AVAL174
APRO175
ATYR212
ASO42720
AHOH2744
AHOH2788

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
DetailsActive site: {}
ChainResidueDetails

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PDB entries from 2025-07-23

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