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1O8U

The 2 Angstrom Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0016823molecular_functionhydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
B0016787molecular_functionhydrolase activity
B0016823molecular_functionhydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
C0016787molecular_functionhydrolase activity
C0016823molecular_functionhydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
D0016787molecular_functionhydrolase activity
D0016823molecular_functionhydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
E0016787molecular_functionhydrolase activity
E0016823molecular_functionhydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
F0016787molecular_functionhydrolase activity
F0016823molecular_functionhydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NA A1253
ChainResidue
AHOH2130
AHOH2131
BASP186
BHOH2123
BHOH2126
CASP186
CHOH2120
CHOH2122

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA D1253
ChainResidue
EASP186
EHOH2129
EHOH2130
FHOH2113
FHOH2115
FHOH2116
DHOH2109

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AGLU124
BGLU124
CGLU124
DGLU124
EGLU124
FGLU124

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:15138275
ChainResidueDetails
ATRP40
CHIS145
CASP154
CGLU244
DTRP40
DHIS145
DASP154
DGLU244
ETRP40
EHIS145
EASP154
AHIS145
EGLU244
FTRP40
FHIS145
FASP154
FGLU244
AASP154
AGLU244
BTRP40
BHIS145
BASP154
BGLU244
CTRP40

218853

PDB entries from 2024-04-24

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