Structure of PDB 4hk6 Chain C

Receptor sequence
>4hk6C (length=374) Species: 73501 (Cordyceps militaris) [Search protein sequence]
PVVVDIHTHMYPPSYIAMLEKRQTIPLVRTFPQADEPRLILLSSELAALD
AALADPAAKLPGRPLSTHFASLAQKMHFMDTNGIRVSVISLANPWFDFLA
PDEAPGIADAVNAEFSDMCAQHVGRLFFFAALPLSAPVDAVKASIERVKN
LKYCRGIILGTSGLGKGLDDPHLLPVFEAVADAKLLVFLHPHYGLPNEVY
GPRSEEYGHVLPLALGFPMETTIAVARMYMAGVFDHVRNLQMLLAHSGGT
LPFLAGRIESCIVHDGHLVKTGKVPKDRRTIWTVLKEQIYLDAVIYSEVG
LQAAIASSGADRLMFGTDHPFFPPIEEDVQGPWDSSRLNAQAVIKAVGEG
SSDAAAVMGLNAVRVLSLKAELEH
3D structure
PDB4hk6 Crystal structures of isoorotate decarboxylases reveal a novel catalytic mechanism of 5-carboxyl-uracil decarboxylation and shed light on the search for DNA decarboxylase.
ChainC
Resolution2.3 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 4.1.1.66: uracil-5-carboxylate decarboxylase.
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 ZN C H12 H14 H195 D323 H7 H9 H190 D318
BS02 5NU C R68 N98 H195 L218 F222 H251 D323 F326 F327 R63 N93 H190 L213 F217 H246 D318 F321 F322
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4hk6, PDBe:4hk6, PDBj:4hk6
PDBsum4hk6
PubMed23917530
UniProtG3J531

[Back to BioLiP]