Structure of PDB 3r7l Chain E

Receptor sequence
>3r7lE (length=290) Species: 1423 (Bacillus subtilis) [Search protein sequence]
MKHLTTMSELSTEEIKDLLQTAQELKSGKTDNQLTGKFAANLFFEPSTRT
RFSFEVAEKKLGMNVLNLDGTSTSVQKGETLYDTIRTLESIGVDVCVIRH
SEDEYYEELVSQVNIPILNAGDGCGQHPTQSLLDLMTIYEEFNTFKGLTV
SIHGDIKHSRVARSNAEVLTRLGARVLFSGPSEWQDEENTFGTYVSMDEA
VESSDVVMLLRIQNERHQSAVSQEGYLNKYGLTVERAERMKRHAIIMHPA
PVNRGVEIDDSLVESEKSRIFKQMKNGVFIRMAVIQRALQ
3D structure
PDB3r7l Crystallographic Snapshots of the Complete Catalytic Cycle of the Unregulated Aspartate Transcarbamoylase from Bacillus subtilis.
ChainE
Resolution2.585 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R49 T50 K77 R99 H127 Q130 L210 P249 G277
Catalytic site (residue number reindexed from 1) R49 T50 K77 R99 H127 Q130 L210 P249 G277
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 PAL E S74 K77 S74 K77
BS02 PAL E S47 T48 R49 T50 R99 H127 R160 V161 R211 A250 S47 T48 R49 T50 R99 H127 R160 V161 R211 A250
Gene Ontology
Molecular Function
GO:0004070 aspartate carbamoyltransferase activity
GO:0016597 amino acid binding
GO:0016740 transferase activity
GO:0016743 carboxyl- or carbamoyltransferase activity
Biological Process
GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
GO:0006221 pyrimidine nucleotide biosynthetic process
GO:0006520 amino acid metabolic process
GO:0044205 'de novo' UMP biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3r7l, PDBe:3r7l, PDBj:3r7l
PDBsum3r7l
PubMed21663747
UniProtP05654|PYRB_BACSU Aspartate carbamoyltransferase catalytic subunit (Gene Name=pyrB)

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