Structure of PDB 2bgm Chain A

Receptor sequence
>2bgmA (length=267) Species: 35933 (Podophyllum peltatum) [Search protein sequence]
TNRLQDKVAIITGGAGGIGETTAKLFVRYGAKVVIADIADDHGQKVCNNI
GSPDVISFVHCDVTKDEDVRNLVDTTIAKHGKLDIMFGNVGVLSTTPYSI
LEAGNEDFKRVMDINVYGAFLVAKHAARVMIPAKKGSIVFTASISSFTAG
EGVSHVYTATKHAVLGLTTSLCTELGEYGIRVNCVSPYIVASPLLTDVFG
VDSSRVEELAHQAANLKGTLLRAEDVADAVAYLAGDESKYVSGLNLVIDG
GYTRTNPAFPTALKHGL
3D structure
PDB2bgm Crystal Structures of Apo-Form and Binary/Ternary Complexes of Podophyllum Secoisolariciresinol Dehydrogenase, an Enzyme Involved in Formation of Health-Protecting and Plant Defense Lignans
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S153 Y167 K171
Catalytic site (residue number reindexed from 1) S143 Y157 K161
Enzyme Commision number 1.1.1.331: secoisolariciresinol dehydrogenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAJ A G23 G26 I28 D47 I48 C71 D72 V73 N99 V100 G101 T151 S153 Y167 K171 V200 G13 G16 I18 D37 I38 C61 D62 V63 N89 V90 G91 T141 S143 Y157 K161 V190
BS02 MAX A L103 S104 I154 G162 V163 S164 Y167 Y198 I199 L93 S94 I144 G152 V153 S154 Y157 Y188 I189
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0102911 (-)-secoisolariciresinol dehydrogenase activity
Biological Process
GO:0009807 lignan biosynthetic process
GO:0051289 protein homotetramerization

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Molecular Function
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Biological Process
External links
PDB RCSB:2bgm, PDBe:2bgm, PDBj:2bgm
PDBsum2bgm
PubMed15653677
UniProtQ94KL8|SILD_PODPE Secoisolariciresinol dehydrogenase (Fragment)

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