Structure of PDB 5epo Chain D

Receptor sequence

>5epoD (length=261) Species: 29369 (Clostridium sardiniense) [Search protein sequence]

MKRLEGKVAIVTSSTRGIGRASAEALAKEGALVYLAARSEELANEVIADI
KKQGGVAKFVYFNAREEETYTSMVEKVAEAEGRIDILVNNYGGTNVNLDK
NLTAGDTDEFFRILKDNVQSVYLPAKAAIPHMEKVGGGSIVNISTIGSVV
PDISRIAYCVSKSAINSLTQNIALQYARKNIRCNAVLPGLIGTRAALENM
TDEFRDSFLGHVPLNRVGRPEDIANAVLYYASDDSGYVTGMIHEVAGGFA
LGTPQYSEYCP

3D structure

PDB

5epo The three-dimensional structure of Clostridium absonum 7 alpha-hydroxysteroid dehydrogenase: new insights into the conserved arginines for NADP(H) recognition

Chain

Resolution

2.0 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	G17 T145 I153 Y158 K162 R194
Catalytic site (residue number reindexed from 1)	G17 T145 I153 Y158 K162 R194
Enzyme Commision number	1.1.1.-

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	NAP	D	S13 T15 R16 G17 I18 R38 F62 N63 A64 N90 Y91 G92 Y158 K162 I191 T193 R194 A195 A196	S13 T15 R16 G17 I18 R38 F62 N63 A64 N90 Y91 G92 Y158 K162 I191 T193 R194 A195 A196
BS02	TUD	D	G93 T94 N95 T145 R155 Y158 G189 N199 M200 F204	G93 T94 N95 T145 R155 Y158 G189 N199 M200 F204

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
GO:0016491	oxidoreductase activity

	Biological Process
GO:0016042	lipid catabolic process
GO:0030573	bile acid catabolic process

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:5epo, PDBe:5epo, PDBj:5epo
PDBsum	5epo
PubMed	26961171
UniProt	G9FRD7\|HDHA_CLOSR 7alpha-hydroxysteroid dehydrogenase (Gene Name=hdha)

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