Structure of PDB 2g7m Chain X

Receptor sequence

>2g7mX (length=321) Species: 817 (Bacteroides fragilis)

GSHMKKFTCVQDIGDLKSALAESFEIKKDRFKYVELGRNKTLLMIFFNSS
LRTRLSTQKAALNLGMNVIVLDINQGAWKLETERGVIMDGDKEEHLLEAI
PVMGCYCDIIGVRSFARFENREYDYNEVIINQFIQHSGRPVFSMEAATRH
PLQSFADLITIEEYKKTARPKVVMTWAPHPRPLPQAVPNSFAEWMNATDY
EFVITHPEGYELDPKFVGNARVEYDQMKAFEGADFIYAKNWAAYLGDNYG
QILSTDRNWTVGDRQMAVTNNAYFMHCLPVRRNMIVTDDVIESPQSIVIP
EAANREISATVVLKRLLENLP

3D structure

• PDB: 2g7m A single mutation in the active site swaps the substrate specificity of N-acetyl-L-ornithine transcarbamylase and N-succinyl-L-ornithine transcarbamylase.
• Chain: X
• Resolution: 2.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R110 H147 Q150 K236 C274 R302
• Catalytic site (residue number reindexed from 1): R113 H150 Q153 K239 C277 R305
• Enzyme Commision number: 2.1.3.11: N-succinylornithine 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	X	E142 K236	E145 K239
BS02	CP	X	S47 L48 R49 T50 R110 L275 R302	S50 L51 R52 T53 R113 L278 R305
BS03	AN0	X	W75 E90	W78 E93

Gene Ontology

Molecular Function

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

External links

• PDB: RCSB:2g7m, PDBe:2g7m, PDBj:2g7m
• PDBsum: 2g7m
• PubMed: 17600144
• UniProt: Q64Z33