Structure of PDB 3b8g Chain A

Receptor sequence
>3b8gA (length=424) Species: 485 (Neisseria gonorrhoeae) [Search protein sequence]
DSFVAHFREAAPYIRQMRGTTLVAGIDGRLLEGGTLNKLAADIGLLSQLG
IRLVLIHGAYHFLDRLAAAQGRTPHYCRGLRVTDETSLGQAQQFAGTVRS
RFEAALCGSSVPLVSGNFLTARPIGVIDGTDMEYAGVIRKTDTAALRFQL
DAGNIVWMPPLGHSYGGKTFNLDMVQAAASVAVSLQAEKLVYLTLSDGIS
RPDGTLAETLSAQEAQSLAEHAASETRRLISSAVAALEGGVHRVQILNGA
ADGSLLQELFTRNGIGTSIAKEAFVSIRQAHSGDIPHIAALIRPLEEQGI
LLHRSREYLENHISEFSILEHDGNLYGCAALKTFAEADCGEIACLAVSPQ
AQDGGYGERLLAHIIDKARGIGISRLFALSTNTGEWFAERGFQTASEDEL
PETRRKDYRSNGRNSHILVRRLHR
3D structure
PDB3b8g The crystal structure of N-acetyl-L-glutamate synthase from Neisseria gonorrhoeae provides insights into mechanisms of catalysis and regulation.
ChainA
Resolution2.6 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 I312 L357 V359 Q364 D365 G367 Y368 G369 E370 S392 T395 E397 W398 I300 L345 V347 Q352 D353 G355 Y356 G357 E358 S380 T383 E385 W386
BS02 NLG 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:3b8g, PDBe:3b8g, PDBj:3b8g
PDBsum3b8g
PubMed18184660
UniProtQ5FAK7

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