Structure of PDB 2i3g Chain B

Receptor sequence
>2i3gB (length=345) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
NATKVAVAGASGYAGGEILRLLLGHPAYADGRLRIGALTAATSAGSTLGE
HHPHLTPLAHRVVEPTEAAVLGGHDAVFLALPHGHSAVLAQQLSPETLII
DCGADFRLTDAAVWERFYGSSHAGSWPYGLPELPGARDQLRGTRRIAVPG
CYPTAALLALFPALAADLIEPAVTVVAVSGTSGAGRAATTDLLGAEVIGS
ARAYNIAGVHRHTPEIAQGLRAVTDRDVSVSFTPVLIPASRGILATCTAR
TRSPLSQLRAAYEKAYHAEPFIYLMPEGQLPRTGAVIGSNAAHIAVAVDE
DAQTFVAIAAIDNLVKGTAGAAVQSMNLALGWPETDGLSVVGVAP
3D structure
PDB2i3g Crystal Structure of N-acetyl-gamma-glutamyl-phosphate Reductase from Mycobacterium tuberculosis in Complex with NADP(+).
ChainB
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 B G16 S18 G19 Y20 A21 A47 A48 S50 T73 A87 L88 P89 C109 G190 G192 R193 L321 T325 G9 S11 G12 Y13 A14 A40 A41 S43 T66 A80 L81 P82 C102 G183 G185 R186 L314 T318
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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