Structure of PDB 2g7m Chain Z Binding Site BS03

Receptor Information
>2g7m Chain Z (length=320) Species: 817 (Bacteroides fragilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SHMKKFTCVQDIGDLKSALAESFEIKKDRFKYVELGRNKTLLMIFFNSSL
RTRLSTQKAALNLGMNVIVLDINQGAWKLETERGVIMDGDKEEHLLEAIP
VMGCYCDIIGVRSFARFENREYDYNEVIINQFIQHSGRPVFSMEAATRHP
LQSFADLITIEEYKKTARPKVVMTWAPHPRPLPQAVPNSFAEWMNATDYE
FVITHPEGYELDPKFVGNARVEYDQMKAFEGADFIYAKNWAAYLGDNYGQ
ILSTDRNWTVGDRQMAVTNNAYFMHCLPVRRNMIVTDDVIESPQSIVIPE
AANREISATVVLKRLLENLP
Ligand information
Ligand IDCP
InChIInChI=1S/CH4NO5P/c2-1(3)7-8(4,5)6/h(H2,2,3)(H2,4,5,6)
InChIKeyFFQKYPRQEYGKAF-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341NC(=O)O[P](O)(O)=O
OpenEye OEToolkits 1.5.0C(=O)(N)OP(=O)(O)O
FormulaC H4 N O5 P
NamePHOSPHORIC ACID MONO(FORMAMIDE)ESTER
ChEMBLCHEMBL369105
DrugBank
ZINCZINC000008383183
PDB chain2g7m Chain Z Residue 546 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2g7m A single mutation in the active site swaps the substrate specificity of N-acetyl-L-ornithine transcarbamylase and N-succinyl-L-ornithine transcarbamylase.
Resolution2.9 Å
Binding residue
(original residue number in PDB)		S47 L48 R49 T50 R110 L275 R302
Binding residue
(residue number reindexed from 1)		S49 L50 R51 T52 R112 L277 R304
Annotation score2
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.
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2g7m, PDBe:2g7m, PDBj:2g7m
PDBsum2g7m
PubMed17600144
UniProtQ64Z33

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