Structure of PDB 3d2p Chain A

Receptor sequence

>3d2pA (length=424) Species: 485 (Neisseria gonorrhoeae)

DSFVAHFREAAPYIRQMRGTTLVAGIDGRLLEGGTLNKLAADIGLLSQLG
IRLVLIHGAYHFLDRLAAAQGRTPHYCRGLRVTDETSLGQAQQFAGTVRS
RFEAALCGSVSGFARAPSVPLVSGNFLTARPIGVIDGTDMEYAGVIRKTD
TAALRFQLDAGNIVWMPPLGHSYGGKTFNLDMVQAAASVAVSLQAEKLVY
LTLSDGISRPDGTLAETLSAQEAQSLAEHAASETRRLISSAVAALEGGVH
RVQILNGAADGSLLQELFTRNGIGTSIAKEAFVSIRQAHSGDIPHIAALI
RPLILLHRSREYLENHISEFSILEHDGNLYGCAALKTFAEADCGEIACLA
VSPQAQDGGYGERLLAHIIDKARGIGISRLFALSTNTGEWFAERGFQTAS
EDELPETRRKDYRNSHILVRRLHR

3D structure

• PDB: 3d2p Mechanism of Allosteric Inhibition of N-Acetyl-L-glutamate Synthase by L-Arginine.
• Chain: A
• Resolution: 2.56 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): I30
• Catalytic site (residue number reindexed from 1): I26
• Enzyme Commision number: 2.3.1.1: amino-acid N-acetyltransferase.

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	COA	A	L307 L357 V359 Q364 D365 G367 G369 E370 E397 W398	L303 L349 V351 Q356 D357 G359 G361 E362 E389 W390
BS02	ARG	A	Y17 K201 E220 Q257 E270 L271 T273 R274 N275 G278 S280	Y13 K197 E216 Q253 E266 L267 T269 R270 N271 G274 S276

Gene Ontology

Molecular Function

• GO:0004042 L-glutamate N-acetyltransferase activity
• GO:0016746 acyltransferase activity
• GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups

Biological Process

• GO:0006526 L-arginine biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:3d2p, PDBe:3d2p, PDBj:3d2p
• PDBsum: 3d2p
• PubMed: 19095660
• UniProt: Q5FAK7