Structure of PDB 2i2x Chain L

Receptor sequence
>2i2xL (length=258) Species: 2208 (Methanosarcina barkeri) [Search protein sequence]
MLDFTEASLKKVLTRYNVALEKALTPEEAAEELYPKDELIYPIAKAIFEG
EEDDVVEGLQAAIEAGKDPIDLIDDALMVGMGVVIRLYDEGVIFLPNVMM
SADAMLEGIEYCKENSGATPKTKGTVVCHVAEGDVHDIGKNIVTALLRAN
GYNVVDLGRDVPAEEVLAAVQKEKPIMLTGTALMTTTMYAFKEVNDMLLE
NGIKIPFACGGGAVNQDFVSQFALGVYGEEAADAPKIADAIIAGTTDVTE
LREKFHKH
3D structure
PDB2i2x Insight into the mechanism of biological methanol activation based on the crystal structure of the methanol-cobalamin methyltransferase complex
ChainL
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D134 H136 T187
Catalytic site (residue number reindexed from 1) D134 H136 T187
Enzyme Commision number 2.1.1.90: methanol--corrinoid protein Co-methyltransferase.
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 B13 L G133 D134 V135 H136 D137 I138 G139 V143 T179 T181 L183 M184 T185 A208 G210 G211 G212 G228 E229 E230 A231 G133 D134 V135 H136 D137 I138 G139 V143 T179 T181 L183 M184 T185 A208 G210 G211 G212 G228 E229 E230 A231
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008168 methyltransferase activity
GO:0008705 methionine synthase activity
GO:0031419 cobalamin binding
GO:0046872 metal ion binding
GO:0050897 cobalt ion binding
Biological Process
GO:0009086 methionine biosynthetic process
GO:0015948 methanogenesis
GO:0046653 tetrahydrofolate metabolic process
GO:0050667 homocysteine metabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2i2x, PDBe:2i2x, PDBj:2i2x
PDBsum2i2x
PubMed17142327
UniProtQ46EH4|MTAC_METBF Methanol--corrinoid protein (Gene Name=mtaC)

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