Structure of PDB 3o2g Chain A

Receptor sequence
>3o2gA (length=386) Species: 9606 (Homo sapiens) [Search protein sequence]
SMACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAK
ARKLLVEALDVNIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQ
ARAKLQRELFFPECQYWGSELQLPTLDFEDVLRYDEHAYKWLSTLKKVGI
VRLTGASDKPGEVSKLGKRMGFLYLTFYGHTWQVQDKIDANNVAYTTGKL
SFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQKLKKNNPQAF
QILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTI
FDVPVERVQPFYAALKEFVDLMNSKESKFTFKMNPGDVITFDNWRLLHGR
RSYEAGTEISRHLEGAYADWDVVMSRLRILRQRVEN
3D structure
PDB3o2g Structural and mechanistic studies on gamma-butyrobetaine hydroxylase.
ChainA
Resolution1.78 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 A H202 D204 H347 H203 D205 H348
BS02 ZN A C38 C40 C43 H82 C39 C41 C44 H83
BS03 NM2 A Y177 W181 N191 Y194 D204 Y205 N292 Y366 Y178 W182 N192 Y195 D205 Y206 N293 Y367
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:3o2g, PDBe:3o2g, PDBj:3o2g
PDBsum3o2g
PubMed21168767
UniProtO75936|BODG_HUMAN Gamma-butyrobetaine dioxygenase (Gene Name=BBOX1)

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