Structure of PDB 4lak Chain A Binding Site BS01

Receptor Information
>4lak Chain A (length=336) Species: 983644 (Cordyceps militaris CM01) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PVVVDIHTHMYPPSYIAMLEKRQTIPLLPGRPLSTHFASLAQKMHFMDTN
GIRVSVISLANPWFDFLAPDEAPGIADAVNAEFSDMCAQHVGRLFFFAAL
PLSAPVDAVKASIERVKNLKYCRGIILGTSGLGKGLDDPHLLPVFEAVAD
AKLLVFLHPHYGLPNEVYGPRSEEYGHVLPLALGFPMETTIAVARMYMAG
VFDHVRNLQMLLAHSGGTLPFLAGRIESCIVHDGHLVKTGKVPKDRRTIW
TVLKEQIYLDAVIYSEVGLQAAIASSGADRLMFGTNHPFFPPIEEDVQGP
WDSSRLNAQAVIKAVGEGSSDAAAVMGLNAVRVLSL
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain4lak Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4lak Crystal structures of isoorotate decarboxylases reveal a novel catalytic mechanism of 5-carboxyl-uracil decarboxylation and shed light on the search for DNA decarboxylase.
Resolution2.41 Å
Binding residue
(original residue number in PDB)
H12 H14 H195 N323
Binding residue
(residue number reindexed from 1)
H7 H9 H158 N286
Annotation score4
Enzymatic activity
Enzyme Commision number ?
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4lak, PDBe:4lak, PDBj:4lak
PDBsum4lak
PubMed23917530
UniProtG3J531

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