Structure of PDB 1duv Chain I

Receptor sequence

>1duvI (length=333) Species: 562 (Escherichia coli)

SGFYHKHFLKLLDFTPAELNSLLQLAAKLKADKKSGKEEAKLTGKNIALI
FEKDSTRTRCSFEVAAYDQGARVTYLGPSGSQIGHKESIKDTARVLGRMY
DGIQYRGYGQEIVETLAEYASVPVWNGLTNEFHPTQLLADLLTMQEHLPG
KAFNEMTLVYAGDARNNMGNSMLEAAALTGLDLRLVAPQACWPEAALVTE
CRALAQQNGGNITLTEDVAKGVEGADFIYTDVWVSMGEAKEKWAERIALL
REYQVNSKMMQLTGNPEVKFLHCLPAFHDDQTTLGKKMAEEFGLHGGMEV
TDEVFESAASIVFDQAENRMHTIKAVMVATLSK

3D structure

• PDB: 1duv Mechanism of inactivation of ornithine transcarbamoylase by Ndelta -(N'-Sulfodiaminophosphinyl)-L-ornithine, a true transition state analogue? Crystal structure and implications for catalytic mechanism.
• Chain: I
• Resolution: 1.7 Å

Enzymatic activity

• Enzyme Commision number: 2.1.3.3: ornithine 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	PSQ	I	S55 T56 R57 T58 R106 L128 H133 Q136 N167 D231 S235 M236 C273 L274 R319	S55 T56 R57 T58 R106 L128 H133 Q136 N167 D231 S235 M236 C273 L274 R319	MOAD: Kd=1.6pM PDBbind-CN: -logKd/Ki=11.80,Kd=1.6pM

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:0046872 metal ion binding

Biological Process

• GO:0006520 amino acid metabolic process
• GO:0006526 L-arginine biosynthetic process
• GO:0006591 ornithine metabolic process
• GO:0019240 citrulline biosynthetic process
• GO:0042450 arginine biosynthetic process via ornithine

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1duv, PDBe:1duv, PDBj:1duv
• PDBsum: 1duv
• PubMed: 10747936
• UniProt: P04391|OTC1_ECOLI Ornithine carbamoyltransferase subunit I (Gene Name=argI)