Structure of PDB 2i3g Chain A

Receptor sequence
>2i3gA (length=347) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
VANATKVAVAGASGYAGGEILRLLLGHPAYADGRLRIGALTAATSAGSTL
GEHHPHLTPLAHRVVEPTEAAVLGGHDAVFLALPHGHSAVLAQQLSPETL
IIDCGADFRLTDAAVWERFYGSSHAGSWPYGLPELPGARDQLRGTRRIAV
PGCYPTAALLALFPALAADLIEPAVTVVAVSGTSGAGRAATTDLLGAEVI
GSARAYNIAGVHRHTPEIAQGLRAVTDRDVSVSFTPVLIPASRGILATCT
ARTRSPLSQLRAAYEKAYHAEPFIYLMPEGQLPRTGAVIGSNAAHIAVAV
DEDAQTFVAIAAIDNLVKGTAGAAVQSMNLALGWPETDGLSVVGVAP
3D structure
PDB2i3g Crystal Structure of N-acetyl-gamma-glutamyl-phosphate Reductase from Mycobacterium tuberculosis in Complex with NADP(+).
ChainA
Resolution1.85 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.2.1.38: N-acetyl-gamma-glutamyl-phosphate 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 NAP A G16 S18 G19 Y20 A21 A47 A48 T49 S50 T73 A87 L88 P89 C109 G190 G192 R193 L321 T325 G11 S13 G14 Y15 A16 A42 A43 T44 S45 T68 A82 L83 P84 C104 G185 G187 R188 L316 T320
Gene Ontology
Molecular Function
GO:0003942 N-acetyl-gamma-glutamyl-phosphate reductase activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0051287 NAD binding
GO:0070401 NADP+ binding
Biological Process
GO:0006526 L-arginine biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2i3g, PDBe:2i3g, PDBj:2i3g
PDBsum2i3g
PubMed17316682
UniProtP9WPZ9|ARGC_MYCTU N-acetyl-gamma-glutamyl-phosphate reductase (Gene Name=argC)

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