Structure of PDB 3kzo Chain A

Receptor sequence

>3kzoA (length=332) Species: 190485 (Xanthomonas campestris pv. campestris str. ATCC 33913)

LKHFLNTQDWSRAELDALLTQAALFKRNKLGSELKGKSIALVFFNPSMRT
RTSFELGAFQLGGHAVVLQPGKDAWPIEFNLGTVMDGDTEEHIAEVARVL
GRYVDLIGVRAFPKFVDWSKDREDQVLKSFAKYSPVPVINMETITHPCQE
LAHALALQEHFGTPDLRGKKYVLTWTYHPKPLNTAVANSALTIATRMGMD
VTLLCPTPDYILDERYMDWAAQNVAESGGSLQVSHDIDSAYAGADVVYAK
SWGALPFFGNWEPEKPIRDQYQHFIVDERKMALTNNGVFSHCLPLRRNVK
ATDAVMDSPNCIAIDEAENRLHVQKAIMAALV

3D structure

• PDB: 3kzo Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis.
• 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	AN0	A	E144 L184 K252	E142 L182 K250
BS02	CP	A	S49 M50 R51 T52 R112 R322	S47 M48 R49 T50 R110 R320

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:3kzo, PDBe:3kzo, PDBj:3kzo
• PDBsum: 3kzo
• PubMed: 16741992
• UniProt: Q8P8J2|AOTC_XANCP N-acetylornithine carbamoyltransferase (Gene Name=argF')