Structure of PDB 3r7d Chain A

Receptor sequence

>3r7dA (length=291) Species: 1423 (Bacillus subtilis)

MKHLTTMSELSTEEIKDLLQTAQELKSGKTDNQLTGKFAANLFFEPSTRT
RFSFEVAEKKLGMNVLNLDGTSTSVQKGETLYDTIRTLESIGVDVCVIRH
SEDEYYEELVSQVNIPILNAGDGCGQHPTQSLLDLMTIYEEFNTFKGLTV
SIHGDIKHSRVARSNAEVLTRLGARVLFSGPSEWQDEENTFGTYVSMDEA
VESSDVVMLLRIQNERHQSAVSQEGYLNKYGLTVERAERMKRHAIIMHPA
PVNRGVEIDDSLVESEKSRIFKQMKNGVFIRMAVIQRALQT

3D structure

• PDB: 3r7d Crystallographic Snapshots of the Complete Catalytic Cycle of the Unregulated Aspartate Transcarbamoylase from Bacillus subtilis.
• Chain: A
• Resolution: 2.196 Å

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	PO4	A	S11 T12 R171	S11 T12 R171
BS02	PO4	A	T73 S74 K77	T73 S74 K77

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

External links

• PDB: RCSB:3r7d, PDBe:3r7d, PDBj:3r7d
• PDBsum: 3r7d
• PubMed: 21663747
• UniProt: P05654|PYRB_BACSU Aspartate carbamoyltransferase catalytic subunit (Gene Name=pyrB)