Structure of PDB 4bhi Chain A

Receptor sequence
>4bhiA (length=385) Species: 9606 (Homo sapiens) [Search protein sequence]
MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKA
RKLLVEALDVNIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQA
RAKLQRELFFPECQYWGSELQLPTLDFEDVLRYDEHAYKWLSTLKKVGIV
RLTGASDKPGEVSKLGKRMGFLYLTFYGHTWQVQDKIDANNVAYTTGKLS
FHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQKLKKNNPQAFQ
ILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIF
DVPVERVQPFYAALKEFVDLMNSKESKFTFKMNPGDVITFDNWRLLHGRR
SYEAGTEISRHLEGAYADWDVVMSRLRILRQRVEN
3D structure
PDB4bhi Targeting Carnitine Biosynthesis: Discovery of New Inhibitors Against Gamma-Butyrobetaine Hydroxylase.
ChainA
Resolution2.15 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 RUJ A Y177 W181 N191 Y194 D204 Y205 N292 Y366 Y177 W181 N191 Y194 D204 Y205 N292 Y366 MOAD: Kd=9.3uM
PDBbind-CN: -logKd/Ki=7.05,IC50=90nM
BS02 ZN A H202 D204 H347 H202 D204 H347
BS03 ZN A C38 C40 C43 H82 C38 C40 C43 H82
BS04 16D A Y75 Y83 Y75 Y83
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:4bhi, PDBe:4bhi, PDBj:4bhi
PDBsum4bhi
PubMed24571165
UniProtO75936|BODG_HUMAN Gamma-butyrobetaine dioxygenase (Gene Name=BBOX1)

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