Structure of PDB 2ozp Chain A

Receptor sequence
>2ozpA (length=342) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
KKTLSIVGASGYAGGEFLRLALSHPYLEVKQVTSRRFAGEPVHFVHPNLR
GRTNLKFVPPEKLEPADILVLALPHGVFAREFDRYSALAPVLVDLSADFR
LKDPELYRRYYGEHPRPDLLGRFVYAVPELYREALKGADWIAGAGCNATA
TLLGLYPLLKAGVLKPTPIFVTLLISTSAGGAEASPASHHPERAGSIRVY
KPTGHRHTAEVVENLPGRPEVHLTAIATDRVRGILMTAQCFVQDGWSERD
VWQAYREAYAGEPFIRLVKQKKGVHRYPDPRFVQGTNYADIGFELEEDTG
RLVVMTAIDNLVKGTAGHALQALNVRMGWPETLGLDFPGLHP
3D structure
PDB2ozp Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (TTHA1904) from Thermus thermophilus
ChainA
Resolution2.01 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.2.1.103: [amino-group carrier protein]-6-phospho-L-2-aminoadipate 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 AZI A Y15 A16 A185 Y12 A13 A182
BS02 AZI A H46 R53 H43 R50
Gene Ontology
Molecular Function
GO:0003942 N-acetyl-gamma-glutamyl-phosphate reductase activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0043870 N-acetyl-gamma-aminoadipyl-phosphate reductase activity
GO:0051287 NAD binding
GO:0070401 NADP+ binding
Biological Process
GO:0006526 L-arginine biosynthetic process
GO:0009085 lysine biosynthetic process
GO:0019878 lysine biosynthetic process via aminoadipic acid
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:2ozp, PDBe:2ozp, PDBj:2ozp
PDBsum2ozp
PubMed
UniProtQ5SH26

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