Structure of PDB 1at1 Chain C

Receptor sequence
>1at1C (length=310) Species: 562 (Escherichia coli) [Search protein sequence]
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFE
ASTRTRLSFQTSMHRLGASVVGFSDSANTSLGKKGETLADTISVISTYVD
AIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQQTEG
RLDNLHVAMVGDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILD
MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEYANVKAQFVLR
ASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALL
ALVLNRDLVL
3D structure
PDB1at1 Crystal structures of phosphonoacetamide ligated T and phosphonoacetamide and malonate ligated R states of aspartate carbamoyltransferase at 2.8-A resolution and neutral pH.
ChainC
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) 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.
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 MLI C R105 R167 R229 Q231 R105 R167 R229 Q231
BS02 PCT C S52 T53 R54 T55 R105 H134 L267 S52 T53 R54 T55 R105 H134 L267
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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Biological Process
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Cellular Component
External links
PDB RCSB:1at1, PDBe:1at1, PDBj:1at1
PDBsum1at1
PubMed2405902
UniProtP0A786|PYRB_ECOLI Aspartate carbamoyltransferase catalytic subunit (Gene Name=pyrB)

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