Structure of PDB 3m4n Chain A

Receptor sequence

>3m4nA (length=332) Species: 340 (Xanthomonas campestris pv. campestris)

LKHFLNTQDWSRAELDALLTQAALFKRNKLGSELKGKSIALVFFNPSMRT
RTSFELGAFQLGGHAVVLQPGKDAWPIEFNLGTVMDGDTEEHIAEVARVL
GRYVDLIGVRAFPKFVDWSKDREDQVLKSFAKYSPVPVINMETITHPCQE
LAHALALQEHFGTPDLRGKKYVLTWTYHPKPLNTAVANSALTIATRMGMD
VTLLCPTPDYILDERYMDWAAQNVAESGGSLQVSHDIDSAYAGADVVYAK
SWGALPFFGNWEPEKPIRDQYQHFIVDERKMALTNNGVFSHCLPLRRNVA
ATDAVMDSPNCIAIDEAENRLHVQKAIMAALV

3D structure

• PDB: 3m4n Reversible post-translational carboxylation modulates the enzymatic activity of N-acetyl-L-ornithine transcarbamylase.
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R112 H148 Q151 K252 C294 R322
• Catalytic site (residue number reindexed from 1): R110 H146 Q149 K250 C292 R320
• Enzyme Commision number: 2.1.3.9: N-acetylornithine carbamoyltransferase.

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	PA9	A	S49 M50 R51 T52 R112 E144 H148 K252 L295	S47 M48 R49 T50 R110 E142 H146 K250 L293

Gene Ontology

Molecular Function

• GO:0004585 ornithine carbamoyltransferase activity
• GO:0016597 amino acid binding
• GO:0016740 transferase activity
• GO:0016743 carboxyl- or carbamoyltransferase activity
• GO:0043857 N-acetylornithine carbamoyltransferase activity

Biological Process

• GO:0006520 amino acid metabolic process
• GO:0006526 L-arginine biosynthetic process
• GO:0019240 citrulline biosynthetic process
• GO:0042450 arginine biosynthetic process via ornithine

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:3m4n, PDBe:3m4n, PDBj:3m4n
• PDBsum: 3m4n
• PubMed: 20695527
• UniProt: Q8P8J2|AOTC_XANCP N-acetylornithine carbamoyltransferase (Gene Name=argF')