Structure of PDB 1nfr Chain C

Receptor sequence
>1nfrC (length=244) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
SGRLTGKVALVSGGARGMGASHVRAMVAEGAKVVFGDILDEEGKAMAAEL
ADAARYVHLDVTQPAQWKAAVDTAVTAFGGLHVLVNNAGILNIGTIEDYA
LTEWQRILDVNLTGVFLGIRAVVKPMKEAGRGSIINISSIEGLAGTVACH
GYTATKFAVRGLTKSTALELGPSGIRVNSIHPGLVKTPMTDWVPEDIFQT
ALGRAAEPVEVSNLVVYLASDESSYSTGAEFVVDGGTVAGLAHN
3D structure
PDB1nfr Directed evolution approach to a structural genomics project: Rv2002 from Mycobacterium tuberculosis
ChainC
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 C G14 R17 G18 M19 D38 L40 L60 D61 V62 N88 A89 I91 I138 S140 Y153 K157 P183 G184 L185 V186 T188 P189 M190 T191 G13 R16 G17 M18 D37 L39 L59 D60 V61 N87 A88 I90 I137 S139 Y152 K156 P182 G183 L184 V185 T187 P188 M189 T190
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1nfr, PDBe:1nfr, PDBj:1nfr
PDBsum1nfr
PubMed12524453
UniProtP9WGT1|HSD_MYCTU 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase (Gene Name=fabG3)

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