Structure of PDB 1lqt Chain B

Receptor sequence

>1lqtB (length=454) Species: 1773 (Mycobacterium tuberculosis)

RPYYIAIVGSGPSAFFAAASLLKAADTTEDLDMAVDMLEMLPTPWGLVRS
GVAPDHPKIKSISKQFEKTAEDPRFRFFGNVVVGEHVQPGELSERYDAVI
YAVGAQSDRMLNIPGEDLPGSIAAVDFVGWYNAHPHFEQVSPDLSGARAV
VIGNGNVALDVARILLTDPDVLARTDIADHALESLRPRGIQEVVIVGRRG
PLQAAFTTLELRELADLDGVDVVIDPAELDGITDEDAAAVGKVCKQNIKV
LRGYADREPRPGHRRMVFRFLTSPIEIKGKRKVERIVLGRNELVSDGSGR
VAAKDTGEREELPAQLVVRSVGYRGVPTPGLPFDDQSGTIPNVGGRINGS
PNEYVVGWIKRGPTGVIGTNKKDAQDTVDTLIKNLGNAKEGAECKSFPDH
ADQVADWLAARQPKLVTSAHWQVIDAFERAAGEPHGRPRVKLASLAELLR
IGLG

3D structure

• PDB: 1lqt A covalent modification of NADP+ revealed by the atomic resolution structure of FprA, a Mycobacterium tuberculosis oxidoreductase.
• Chain: B
• Resolution: 1.05 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H57 D161 I368 G369
• Catalytic site (residue number reindexed from 1): H56 D160 I367 G368
• Enzyme Commision number: 1.18.1.2: ferredoxin--NADP(+) reductase.

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	FAD	B	V9 G10 P13 S14 E40 M41 G47 L48 G52 V53 V84 A103 V104 G105 V158 Y324 G358 W359 G366 V367 I368 N371	V8 G9 P12 S13 E39 M40 G46 L47 G51 V52 V83 A102 V103 G104 V157 Y323 G357 W358 G365 V366 I367 N370
BS02	ODP	B	H57 R110 N155 G156 N157 V158 D161 R199 R200 E211 V322 W359 G366	H56 R109 N154 G155 N156 V157 D160 R198 R199 E210 V321 W358 G365

Gene Ontology

Molecular Function

• GO:0004324 ferredoxin-NADP+ reductase activity
• GO:0008860 ferredoxin-NAD+ reductase activity
• GO:0016491 oxidoreductase activity
• GO:0050660 flavin adenine dinucleotide binding
• GO:0070401 NADP+ binding

Cellular Component

• GO:0009274 peptidoglycan-based cell wall

External links

• PDB: RCSB:1lqt, PDBe:1lqt, PDBj:1lqt
• PDBsum: 1lqt
• PubMed: 12102623
• UniProt: P9WIQ3|FPRA_MYCTU NADPH-ferredoxin reductase FprA (Gene Name=fprA)