Structure of PDB 5h8i Chain F Binding Site BS01

Receptor Information

>5h8i Chain F (length=298) Species: 3880 (Medicago truncatula)

DKGRKVVVSALQFACTDDVSTNVTTAERLVRAAHKQGANIVLIQELFEGY
YFCQAQREDFIQRAKPYKDHPTIMRLQKLAKELGVVIPVSFFEEANNAHY
NSIAIIDADGTDLGIYRKSHIPDGPGYEEKFYFNPGDTGFKVFQTKYAKI
GVAICWDQWFPEAARAMALQGAEILFYPTAIGSEPHDQSIDSRDHWKRVM
QGHAGANLVPLVASNRIGNEIIETEHGKSEIKFYGNSFIAGPTGEIVSIA
DDKEEAVLIAEFNLDKIKSMRHCWGVFRDRRPDLYKVLLTLDGKNPVL

Ligand information

• Ligand ID: N2H
• InChI: InChI=1S/C5H14N2O2/c6-3-1-2-4-7-5(8)9/h5,7-9H,1-4,6H2
• InChIKey: JXQFUOSMIWOVKO-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.385: NCCCCNC(O)O
  OpenEye OEToolkits 2.0.4: C(CCNC(O)O)CN
• Formula: C5 H14 N2 O2
• Name: (4-azanylbutylamino)methanediol;
  N-(dihydroxymethyl)putrescine
• ZINC: ZINC000584905780
• PDB chain: 5h8i Chain F Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5h8i Structural Investigations of N-carbamoylputrescine Amidohydrolase from Medicago truncatula: Insights into the Ultimate Step of Putrescine Biosynthesis in Plants.
• Resolution: 1.97 Å
• Binding residue (original residue number in PDB): E48 Y54 Y130 C158 W159 A183 E187
• Binding residue (residue number reindexed from 1): E45 Y51 Y127 C155 W156 A180 E184
• Annotation score: 2

Enzymatic activity

• Catalytic site (original residue number in PDB): E48 N104 K121 E132 C158 A183
• Catalytic site (residue number reindexed from 1): E45 N101 K118 E129 C155 A180
• Enzyme Commision number: 3.5.1.53: N-carbamoylputrescine amidase.

Gene Ontology

Molecular Function

• GO:0016787 hydrolase activity
• GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
• GO:0050126 N-carbamoylputrescine amidase activity

Biological Process

• GO:0006596 polyamine biosynthetic process
• GO:0033388 putrescine biosynthetic process from arginine

External links

• PDB: RCSB:5h8i, PDBe:5h8i, PDBj:5h8i
• PDBsum: 5h8i
• PubMed: 27066023
• UniProt: G7ITU5