Structure of PDB 4c8r Chain F

Receptor sequence
>4c8rF (length=384) Species: 9606 (Homo sapiens) [Search protein sequence]
MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKA
RKLLVEALDVNIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQA
RAKLQRELFFPECQYWGSELQLPTLDFEDVLRYDEHAYKWLSTLKKVGIV
RLTGASDKPGEVSKLGKRMGFLYLTFYGHTWQVQDKIDANNVAYTTGKLS
FHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQKLKKNNPQAFQ
ILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIF
DVPVERVQPFYAALKEFVDLMNSKESKFTFKMNPGDVITFDNWRLLHGRR
SYEAGTEISRHLEGAYADWDVVMSRLRILRQRVE
3D structure
PDB4c8r Modulating carnitine levels by targeting its biosynthesis pathway - selective inhibition of gamma-butyrobetaine hydroxylase.
ChainF
Resolution2.82 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.11.1: gamma-butyrobetaine dioxygenase.
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 F C38 C40 H82 C38 C40 H82
BS02 6YT F H202 L217 S229 H347 R349 R360 H202 L217 S229 H347 R349 R360
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0008336 gamma-butyrobetaine dioxygenase activity
GO:0016491 oxidoreductase activity
GO:0016706 2-oxoglutarate-dependent dioxygenase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0045329 carnitine biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4c8r, PDBe:4c8r, PDBj:4c8r
PDBsum4c8r
PubMed26682037
UniProtO75936|BODG_HUMAN Gamma-butyrobetaine dioxygenase (Gene Name=BBOX1)

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