Structure of PDB 2fg7 Chain D

Receptor sequence

>2fg7D (length=320) Species: 272559 (Bacteroides fragilis NCTC 9343)

SHMKKFTCVQDIGDLKSALAESFEIKKDRFKYVELGRNKTLLMIFFNSSL
RTRLSTQKAALNLGMNVIVLDINQGAWKLETERGVIMDGDKPEHLLEAIP
VMGCYCDIIGVRSFARFENREYDYNEVIINQFIQHSGRPVFSMEAATRHP
LQSFADLITIEEYKKTARPKVVMTWAPHPRPLPQAVPNSFAEWMNATDYE
FVITHPEGYELDPKFVGNARVEYDQMKAFEGADFIYAKNWAAYLGDNYGQ
ILSTDRNWTVGDRQMAVTNNAYFMHCLPVRRNMIVTDDVIESPQSIVIPE
AANREISATVVLKRLLENLP

3D structure

• PDB: 2fg7 Structure and catalytic mechanism of a novel N-succinyl-L-ornithine transcarbamylase in arginine biosynthesis of Bacteroides fragilis.
• Chain: D
• 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	SN0	D	F112 E142 H176 R178 L180 K236 R278	F114 E144 H178 R180 L182 K238 R280
BS02	CP	D	S47 L48 R49 T50 R110 L275 R302	S49 L50 R51 T52 R112 L277 R304
BS03	SN0	D	W75 P90	W77 P92

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:2fg7, PDBe:2fg7, PDBj:2fg7
• PDBsum: 2fg7
• PubMed: 16704984
• UniProt: Q5LI27