2JBW

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0009820	biological_process	alkaloid metabolic process
A	0016787	molecular_function	hydrolase activity
A	0019608	biological_process	nicotine catabolic process
B	0009820	biological_process	alkaloid metabolic process
B	0016787	molecular_function	hydrolase activity
B	0019608	biological_process	nicotine catabolic process
C	0009820	biological_process	alkaloid metabolic process
C	0016787	molecular_function	hydrolase activity
C	0019608	biological_process	nicotine catabolic process
D	0009820	biological_process	alkaloid metabolic process
D	0016787	molecular_function	hydrolase activity
D	0019608	biological_process	nicotine catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A1368

Chain	Residue
A	LEU200
A	THR201
A	LEU203
A	ILE206
A	ASN208

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA B1367

Chain	Residue
B	ASN208
B	HOH2096
B	LEU200
B	THR201
B	LEU203
B	ILE206

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA C1367

Chain	Residue
C	LEU200
C	THR201
C	LEU203
C	ILE206
C	ASN208
C	HOH2167

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site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA D1367

Chain	Residue
D	LEU200
D	LEU203
D	ILE206
D	ASN208

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17275835","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Active site: {"evidences":[{"source":"PubMed","id":"17275835","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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