Structure of PDB 4bhf Chain A

Receptor sequence

>4bhfA (length=384) Species: 9606 (Homo sapiens)

MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKA
RKLLVEALDVNIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQA
RAKLQRELFFPECQYWGSELQLPTLDFEDVLRYDEHAYKWLSTLKKVGIV
RLTGASDKPGEVSKLGKRMGFLYLTFYGHTWQVQDKIDANNVAYTTGKLS
FHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQKLKKNNPQAFQ
ILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIF
DVPVERVQPFYAALKEFVDLMNSKESKFTFKMNPGDVITFDNWRLLHGRR
SYEAGTEISRHLEGAYADWDVVMSRLRILRQRVE

3D structure

• PDB: 4bhf Targeting Carnitine Biosynthesis: Discovery of New Inhibitors Against Gamma-Butyrobetaine Hydroxylase.
• Chain: A
• Resolution: 2.05 Å

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	MZT	A	Y177 W181 N191 Y194 D204 Y205 N292 Y366	Y177 W181 N191 Y194 D204 Y205 N292 Y366	MOAD: Kd=4.1uM PDBbind-CN: -logKd/Ki=3.46,IC50=343uM
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

External links

• PDB: RCSB:4bhf, PDBe:4bhf, PDBj:4bhf
• PDBsum: 4bhf
• PubMed: 24571165
• UniProt: O75936|BODG_HUMAN Gamma-butyrobetaine dioxygenase (Gene Name=BBOX1)