Structure of PDB 3d2m Chain A

Receptor sequence
>3d2mA (length=424) Species: 242231 (Neisseria gonorrhoeae FA 1090) [Search protein sequence]
DSFVAHFREAAPYIRQMRGTTLVAGIDGRLLEGGTLNKLAADIGLLSQLG
IRLVLIHGAYHFLDRLAAAQGRTPHYCRGLRVTDETSLGQAQQFAGTVRS
RFEAALCGSSVPLVSGNFLTARPIGVIDGTDMEYAGVIRKTDTAALRFQL
DAGNIVWMPPLGHSYGGKTFNLDMVQAAASVAVSLQAEKLVYLTLSDGIS
RPDGTLAETLSAQEAQSLAEHAASETRRLISSAVAALEGGVHRVQILNGA
ADGSLLQELFTRNGIGTSIAKEAFVSIRQAHSGDIPHIAALIRPLEEQGI
LLHRSREYLENHISEFSILEHDGNLYGCAALKTFAEADCGEIACLAVSPQ
AQDGGYGERLLAHIIDKARGIGISRLFALSTNTGEWFAERGFQTASEDEL
PETRRKDYRSNGRNSHILVRRLHR
3D structure
PDB3d2m Mechanism of Allosteric Inhibition of N-Acetyl-L-glutamate Synthase by L-Arginine.
ChainA
Resolution2.21 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 L357 V359 Q364 D365 G367 G369 E370 S392 T395 W398 L345 V347 Q352 D353 G355 G357 E358 S380 T383 W386
BS02 GLU A L314 R316 A355 C356 L391 R425 S427 L302 R304 A343 C344 L379 R413 S415
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3d2m, PDBe:3d2m, PDBj:3d2m
PDBsum3d2m
PubMed19095660
UniProtQ5FAK7

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