Structure of PDB 6jks Chain C Binding Site BS01

Receptor Information

>6jks Chain C (length=306) Species: 353153 (Trypanosoma cruzi strain CL Brener)

GSMLELPPVASLKGKSITSAEQFSRADIYALIHLASAMQRKIDAGEVLNL
LQGRIMTPLFFEDSSRTFSSFCAAMIRLGGSVVNFKVEASSINKGETLAD
TIRTLDSYSDVLVMRHPRQDAIEEALSVAQHPILNAGNGAGEHPTQALLD
TLTIHSELGSVDGITIALIGDLKMGRTVHSLLKLLVRNFSIKCVFLVAPD
ALQMPQDVLEPLQHEIATKGVIIHRTHALTDEVMQKSDVLYTTRLQDITI
DAARMRLAKEKMIVMHPLPRNDELSTTVDADPRAAYFRQMRYGMFMRMAI
LWSVLA

Ligand information

• Ligand ID: CP
• InChI: InChI=1S/CH4NO5P/c2-1(3)7-8(4,5)6/h(H2,2,3)(H2,4,5,6)
• InChIKey: FFQKYPRQEYGKAF-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: NC(=O)O[P](O)(O)=O
  OpenEye OEToolkits 1.5.0: C(=O)(N)OP(=O)(O)O
• Formula: C H4 N O5 P
• Name: PHOSPHORIC ACID MONO(FORMAMIDE)ESTER
• ChEMBL: CHEMBL369105
• ZINC: ZINC000008383183
• PDB chain: 6jks Chain C Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6jks Crystallographic snapshots of Trypanosoma cruzi aspartate transcarbamoylase revealed an ordered Bi-Bi reaction mechanism
• Resolution: 2.1 Å
• Binding residue (original residue number in PDB): S62 S63 R64 T65 R113 H141 P287 L288
• Binding residue (residue number reindexed from 1): S64 S65 R66 T67 R115 H143 P267 L268
• Annotation score: 2

Enzymatic activity

• Catalytic site (original residue number in PDB): R113 H141 Q144 T241 P287 G313
• Catalytic site (residue number reindexed from 1): R115 H143 Q146 T243 P267 G293
• Enzyme Commision number: 2.1.3.2: aspartate carbamoyltransferase.

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:6jks, PDBe:6jks, PDBj:6jks
• PDBsum: 6jks
• UniProt: Q4D3W3