Structure of PDB 8gju Chain K

Receptor sequence
>8gjuK (length=686) Species: 9606 (Homo sapiens) [Search protein sequence]
QQPLHPEWAALAKKQLKNPEDLIWHTPEGISIKPLYSKRDTMDLPEELPG
VKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVA
FDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMT
MNGAVIPVLANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEP
SMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEY
SRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMF
QPKNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHT
NSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTND
VYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIV
GVNKYQLEKEDTVEVLAIDNTSVRNRQIEKLKKIKSSRDQALAERCLAAL
TECAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKEITSAIKRVH
KFMEREGRRPRLLVAKMGQDRGAKVIATGFADLGFDVDIGPLFQTPREVA
QQAVDADVHAVGVSTLAAGHKTLVPELIKELNSLGRPDILVMCGGVIPPQ
DYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLE
3D structure
PDB8gju Architecture of the human G-protein-methylmalonyl-CoA mutase nanoassembly for B 12 delivery and repair.
ChainK
Resolution2.79 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 5.4.99.2: methylmalonyl-CoA mutase.
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 COA K Y96 T98 M99 R103 T106 R108 S185 M186 T187 T216 Q218 N257 S260 R304 R348 A349 H350 Q383 Y59 T61 M62 R66 T69 R71 S148 M149 T150 T179 Q181 N220 S223 R267 R311 A312 H313 Q346
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003924 GTPase activity
GO:0004494 methylmalonyl-CoA mutase activity
GO:0005515 protein binding
GO:0016853 isomerase activity
GO:0016866 intramolecular transferase activity
GO:0031419 cobalamin binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0072341 modified amino acid binding
Biological Process
GO:0006790 sulfur compound metabolic process
GO:0009791 post-embryonic development
GO:0019678 propionate metabolic process, methylmalonyl pathway
GO:0043547 positive regulation of GTPase activity
GO:0050667 homocysteine metabolic process
GO:1901290 succinyl-CoA biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8gju, PDBe:8gju, PDBj:8gju
PDBsum8gju
PubMed37468522
UniProtP22033|MUTA_HUMAN Methylmalonyl-CoA mutase, mitochondrial (Gene Name=MMUT)

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