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Structure of PDB 2fg6 Chain X

Receptor sequence
>2fg6X (length=322) Species: 272559 (Bacteroides fragilis NCTC 9343) [Search protein sequence]
RGSHMKKFTCVQDIGDLKSALAESFEIKKDRFKYVELGRNKTLLMIFFNS
SLRTRLSTQKAALNLGMNVIVLDINQGAWKLETERGVIMDGDKPEHLLEA
IPVMGCYCDIIGVRSFARFENREYDYNEVIINQFIQHSGRPVFSMEAATR
HPLQSFADLITIEEYKKTARPKVVMTWAPHPRPLPQAVPNSFAEWMNATD
YEFVITHPEGYELDPKFVGNARVEYDQMKAFEGADFIYAKNWAAYLGDNY
GQILSTDRNWTVGDRQMAVTNNAYFMHCLPVRRNMIVTDDVIESPQSIVI
PEAANREISATVVLKRLLENLP
3D structure
PDB2fg6 Structure and catalytic mechanism of a novel N-succinyl-L-ornithine transcarbamylase in arginine biosynthesis of Bacteroides fragilis.
ChainX
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K236
Catalytic site (residue number reindexed from 1) K240
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 SO4 X S47 L48 R49 T50 R110 S51 L52 R53 T54 R114
BS02 SN0 X F112 E142 H176 R178 L180 K236 R278 F116 E146 H180 R182 L184 K240 R282
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

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Molecular Function
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Biological Process
External links

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