Structure of PDB 1duv Chain H

Receptor sequence

>1duvH (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: H
• 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	H	S55 T56 R57 T58 R106 L128 H133 N167 D231 S235 M236 C273 L274 R319	S55 T56 R57 T58 R106 L128 H133 N167 D231 S235 M236 C273 L274 R319	MOAD: 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)