Structure of PDB 1nfr Chain D

Receptor sequence

>1nfrD (length=244) Species: 1773 (Mycobacterium tuberculosis)

SGRLTGKVALVSGGARGMGASHVRAMVAEGAKVVFGDILDEEGKAMAAEL
ADAARYVHLDVTQPAQWKAAVDTAVTAFGGLHVLVNNAGILNIGTIEDYA
LTEWQRILDVNLTGVFLGIRAVVKPMKEAGRGSIINISSIEGLAGTVACH
GYTATKFAVRGLTKSTALELGPSGIRVNSIHPGLVKTPMTDWVPEDIFQT
ALGRAAEPVEVSNLVVYLASDESSYSTGAEFVVDGGTVAGLAHN

3D structure

• PDB: 1nfr Directed evolution approach to a structural genomics project: Rv2002 from Mycobacterium tuberculosis
• Chain: D
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): G18 S140 Y153 K157
• Catalytic site (residue number reindexed from 1): G17 S139 Y152 K156
• Enzyme Commision number: 1.1.1.53: 3alpha(or 20beta)-hydroxysteroid 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	NAD	D	G14 R17 G18 M19 D38 L40 L60 D61 V62 N88 A89 G90 I91 I138 S140 Y153 K157 P183 V186 T188 P189 M190	G13 R16 G17 M18 D37 L39 L59 D60 V61 N87 A88 G89 I90 I137 S139 Y152 K156 P182 V185 T187 P188 M189

Gene Ontology

Molecular Function

• GO:0016491 oxidoreductase activity
• GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
• GO:0047044 androstan-3-alpha,17-beta-diol dehydrogenase activity

Biological Process

• GO:0006706 steroid catabolic process
• GO:0008202 steroid metabolic process

Cellular Component

• GO:0005886 plasma membrane

External links

• PDB: RCSB:1nfr, PDBe:1nfr, PDBj:1nfr
• PDBsum: 1nfr
• PubMed: 12524453
• UniProt: P9WGT1|HSD_MYCTU 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase (Gene Name=fabG3)