Structure of PDB 2otc Chain D

Receptor sequence

>2otcD (length=333) Species: 469008 (Escherichia coli BL21(DE3))

SGFYHKHFLKLLDFTPAELNSLLQLAAKLKADKKSGKEEAKLTGKNIALI
FEKDSTRTRCSFEVAAYDQGARVTYLGPSGSQIGHKESIKDTARVLGRMY
DGIQYRGYGQEIVETLAEYARVPVWNGLTNEFHPTQLLADLLTMQEHLPG
KAFNEMTLVYAGDARNNMGNSMLEAAALTGLDLRLVAPQACWPEAALVTE
CRALAQQNGGNITLTEDVAKGVEGADFIYTDVWVSMGEAKEKWAERIALL
REYQVNSKMMQLTGNPEVKFLHCLPAFHDDQTTLGKKMAEEFGLHGGMEV
TDEVFESAASIVFDQAENRMHTIKAVMVATLSK

3D structure

• PDB: 2otc Substrate-induced conformational change in a trimeric ornithine transcarbamoylase.
• Chain: D
• Resolution: 2.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R57 T58 H85 R106 H133 Q136 D231 C273 R319
• Catalytic site (residue number reindexed from 1): R57 T58 H85 R106 H133 Q136 D231 C273 R319
• 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	PAO	D	S55 T56 R57 T58 R106 H133 N167 D231 S235 M236 L274 R319	S55 T56 R57 T58 R106 H133 N167 D231 S235 M236 L274 R319

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:2otc, PDBe:2otc, PDBj:2otc
• PDBsum: 2otc
• PubMed: 9275160
• UniProt: P04391|OTC1_ECOLI Ornithine carbamoyltransferase subunit I (Gene Name=argI)