Structure of PDB 2r98 Chain A

Receptor sequence

>2r98A (length=424) Species: 485 (Neisseria gonorrhoeae)

DSFVAHFREAAPYIRQMRGTTLVAGIDGRLLEGGTLNKLAADIGLLSQLG
IRLVLIHGAYHFLDRLAAAQGRTPHYCRGLRVTDETSLGQAQQFAGTVRS
RFEAALCGSSVPLVSGNFLTARPIGVIDGTDMEYAGVIRKTDTAALRFQL
DAGNIVWMPPLGHSYGGKTFNLDMVQAAASVAVSLQAEKLVYLTLSDGIS
RPDGTLAETLSAQEAQSLAEHAASETRRLISSAVAALEGGVHRVQILNGA
ADGSLLQELFTRNGIGTSIAKEAFVSIRQAHSGDIPHIAALIRPLEEQGI
LLHRSREYLENHISEFSILEHDGNLYGCAALKTFAEADCGEIACLAVSPQ
AQDGGYGERLLAHIIDKARGIGISRLFALSTNTGEWFAERGFQTASEDEL
PETRRKDYRSNGRNSHILVRRLHR

3D structure

• PDB: 2r98 The crystal structure of N-acetyl-L-glutamate synthase from Neisseria gonorrhoeae provides insights into mechanisms of catalysis and regulation.
• Chain: A
• Resolution: 2.4 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	ACO	A	L307 I312 L357 V359 Q364 D365 G367 G369 E370 S392 T395 E397 W398 F399	L295 I300 L345 V347 Q352 D353 G355 G357 E358 S380 T383 E385 W386 F387

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:2r98, PDBe:2r98, PDBj:2r98
• PDBsum: 2r98
• PubMed: 18184660
• UniProt: Q5FAK7