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2JBW

Crystal Structure of the 2,6-dihydroxy-pseudo-oxynicotine Hydrolase.

Functional Information from GO Data
ChainGOidnamespacecontents
A0009820biological_processalkaloid metabolic process
A0016787molecular_functionhydrolase activity
A0019608biological_processnicotine catabolic process
B0009820biological_processalkaloid metabolic process
B0016787molecular_functionhydrolase activity
B0019608biological_processnicotine catabolic process
C0009820biological_processalkaloid metabolic process
C0016787molecular_functionhydrolase activity
C0019608biological_processnicotine catabolic process
D0009820biological_processalkaloid metabolic process
D0016787molecular_functionhydrolase activity
D0019608biological_processnicotine catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A1368
ChainResidue
ALEU200
ATHR201
ALEU203
AILE206
AASN208

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B1367
ChainResidue
BASN208
BHOH2096
BLEU200
BTHR201
BLEU203
BILE206

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA C1367
ChainResidue
CLEU200
CTHR201
CLEU203
CILE206
CASN208
CHOH2167

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA D1367
ChainResidue
DLEU200
DLEU203
DILE206
DASN208

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255, ECO:0000303|PubMed:17275835
ChainResidueDetails
AGLU148
BGLU148
CGLU148
DGLU148

site_idSWS_FT_FI2
Number of Residues12
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:17275835
ChainResidueDetails
ASER217
DSER217
DASP300
DHIS329
AASP300
AHIS329
BSER217
BASP300
BHIS329
CSER217
CASP300
CHIS329

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PDB entries from 2024-07-10

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