Structure of PDB 4hk5 Chain D Binding Site BS02

Receptor Information

>4hk5 Chain D (length=380) Species: 73501 (Cordyceps militaris)

TPVVVDIHTHMYPPSYIAMLEKRQTIPLVRTFPQADEPRLILLSSELAAL
DAALADPAAKLPGRPLSTHFASLAQKMHFMDTNGIRVSVISLANPWFDFL
APDEAPGIADAVNAEFSDMCAQHVGRLFFFAALPLSAPVDAVKASIERVK
NLKYCRGIILGTSGLGKGLDDPHLLPVFEAVADAKLLVFLHPHYGLPNEV
YGPRSEEYGHVLPLALGFPMETTIAVARMYMAGVFDHVRNLQMLLAHSGG
TLPFLAGRIESCIVHDGHLVKTGKVPKDRRTIWTVLKEQIYLDAVIYSEV
GLQAAIASSGADRLMFGTDHPFFPPIEEDVQGPWDSSRLNAQAVIKAVGE
GSSDAAAVMGLNAVRVLSLKAELEHHHHHH

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 4hk5 Chain D Residue 402

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4hk5 Crystal structures of isoorotate decarboxylases reveal a novel catalytic mechanism of 5-carboxyl-uracil decarboxylation and shed light on the search for DNA decarboxylase.
• Resolution: 1.9 Å
• Binding residue (original residue number in PDB): H379 H384
• Binding residue (residue number reindexed from 1): H375 H380
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 4.1.1.66: uracil-5-carboxylate decarboxylase.

Gene Ontology

Molecular Function

• GO:0016787 hydrolase activity
• GO:0016831 carboxy-lyase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0019748 secondary metabolic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:4hk5, PDBe:4hk5, PDBj:4hk5
• PDBsum: 4hk5
• PubMed: 23917530
• UniProt: G3J531