Structure of PDB 2g7m Chain Z

Receptor sequence

>2g7mZ (length=320) Species: 817 (Bacteroides fragilis)

SHMKKFTCVQDIGDLKSALAESFEIKKDRFKYVELGRNKTLLMIFFNSSL
RTRLSTQKAALNLGMNVIVLDINQGAWKLETERGVIMDGDKEEHLLEAIP
VMGCYCDIIGVRSFARFENREYDYNEVIINQFIQHSGRPVFSMEAATRHP
LQSFADLITIEEYKKTARPKVVMTWAPHPRPLPQAVPNSFAEWMNATDYE
FVITHPEGYELDPKFVGNARVEYDQMKAFEGADFIYAKNWAAYLGDNYGQ
ILSTDRNWTVGDRQMAVTNNAYFMHCLPVRRNMIVTDDVIESPQSIVIPE
AANREISATVVLKRLLENLP

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: Z
• 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): R112 H149 Q152 K238 C276 R304
• 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	Z	W75 E90	W77 E92
BS02	AN0	Z	F112 E142 L180 P181 K236	F114 E144 L182 P183 K238
BS03	CP	Z	S47 L48 R49 T50 R110 L275 R302	S49 L50 R51 T52 R112 L277 R304

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