Structure of PDB 2fg7 Chain Y Binding Site BS02

Receptor Information

>2fg7 Chain Y (length=321) Species: 272559 (Bacteroides fragilis NCTC 9343)

GSHMKKFTCVQDIGDLKSALAESFEIKKDRFKYVELGRNKTLLMIFFNSS
LRTRLSTQKAALNLGMNVIVLDINQGAWKLETERGVIMDGDKPEHLLEAI
PVMGCYCDIIGVRSFARFENREYDYNEVIINQFIQHSGRPVFSMEAATRH
PLQSFADLITIEEYKKTARPKVVMTWAPHPRPLPQAVPNSFAEWMNATDY
EFVITHPEGYELDPKFVGNARVEYDQMKAFEGADFIYAKNWAAYLGDNYG
QILSTDRNWTVGDRQMAVTNNAYFMHCLPVRRNMIVTDDVIESPQSIVIP
EAANREISATVVLKRLLENLP

Ligand information

• Ligand ID: CP
• InChI: InChI=1S/CH4NO5P/c2-1(3)7-8(4,5)6/h(H2,2,3)(H2,4,5,6)
• InChIKey: FFQKYPRQEYGKAF-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: NC(=O)O[P](O)(O)=O
  OpenEye OEToolkits 1.5.0: C(=O)(N)OP(=O)(O)O
• Formula: C H4 N O5 P
• Name: PHOSPHORIC ACID MONO(FORMAMIDE)ESTER
• ChEMBL: CHEMBL369105
• ZINC: ZINC000008383183
• PDB chain: 2fg7 Chain Y Residue 348

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2fg7 Structure and catalytic mechanism of a novel N-succinyl-L-ornithine transcarbamylase in arginine biosynthesis of Bacteroides fragilis.
• Resolution: 2.9 Å
• Binding residue (original residue number in PDB): S47 L48 R49 T50 R110 C274 L275 R302
• Binding residue (residue number reindexed from 1): S50 L51 R52 T53 R113 C277 L278 R305
• Annotation score: 2

Enzymatic activity

• Catalytic site (original residue number in PDB): K236
• Catalytic site (residue number reindexed from 1): K239
• Enzyme Commision number: 2.1.3.11: N-succinylornithine carbamoyltransferase.

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