Structure of PDB 1at1 Chain A Binding Site BS02
Receptor Information
>1at1 Chain A (length=310) Species:
562
(Escherichia coli) [
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ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFE
ASTRTRLSFQTSMHRLGASVVGFSDSANTSLGKKGETLADTISVISTYVD
AIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQQTEG
RLDNLHVAMVGDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILD
MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEYANVKAQFVLR
ASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALL
ALVLNRDLVL
Ligand information
Ligand ID
PCT
InChI
InChI=1S/C2H6NO4P/c3-2(4)1-8(5,6)7/h1H2,(H2,3,4)(H2,5,6,7)
InChIKey
AKVIWWJLBFWFLM-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
O=C(N)CP(=O)(O)O
OpenEye OEToolkits 1.5.0
C(C(=O)N)P(=O)(O)O
CACTVS 3.341
NC(=O)C[P](O)(O)=O
Formula
C2 H6 N O4 P
Name
PHOSPHONOACETAMIDE
ChEMBL
DrugBank
ZINC
PDB chain
1at1 Chain A Residue 311 [
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Receptor-Ligand Complex Structure
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PDB
1at1
Crystal structures of phosphonoacetamide ligated T and phosphonoacetamide and malonate ligated R states of aspartate carbamoyltransferase at 2.8-A resolution and neutral pH.
Resolution
2.8 Å
Binding residue
(original residue number in PDB)
S52 T53 R54 T55 R105 H134 Q137
Binding residue
(residue number reindexed from 1)
S52 T53 R54 T55 R105 H134 Q137
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
R54 T55 K84 R105 H134 Q137 T228 P266 G292
Catalytic site (residue number reindexed from 1)
R54 T55 K84 R105 H134 Q137 T228 P266 G292
Enzyme Commision number
2.1.3.2
: aspartate carbamoyltransferase.
Gene Ontology
Molecular Function
GO:0004070
aspartate carbamoyltransferase activity
GO:0004088
carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
GO:0005515
protein binding
GO:0016597
amino acid binding
GO:0016740
transferase activity
GO:0016743
carboxyl- or carbamoyltransferase activity
GO:0042802
identical protein binding
Biological Process
GO:0006207
'de novo' pyrimidine nucleobase biosynthetic process
GO:0006221
pyrimidine nucleotide biosynthetic process
GO:0006520
amino acid metabolic process
GO:0006541
glutamine metabolic process
GO:0044205
'de novo' UMP biosynthetic process
GO:0070207
protein homotrimerization
Cellular Component
GO:0005737
cytoplasm
GO:0005829
cytosol
GO:0009347
aspartate carbamoyltransferase complex
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Molecular Function
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Cellular Component
External links
PDB
RCSB:1at1
,
PDBe:1at1
,
PDBj:1at1
PDBsum
1at1
PubMed
2405902
UniProt
P0A786
|PYRB_ECOLI Aspartate carbamoyltransferase catalytic subunit (Gene Name=pyrB)
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