Structure of PDB 2qbu Chain B

Receptor sequence
>2qbuB (length=228) Species: 187420 (Methanothermobacter thermautotrophicus str. Delta H) [Search protein sequence]
MHGKLIGVGVGPGDSELLTLRAVNVLRSVPVICAPRSSSERESIALSIVE
DILTERRDGCRILDPVFPMTDDRDELESHWDSAARMVAAELEDGRDVAFI
TLGDPSIYSTFSYLQQRIEDMGFKTEMVPGVTSFTACAATAGRTLVEGDE
ILLVVPRVDDRFERVLRDVDACVIMKTSRHGRRAMEVVESDPRGKDVVSV
ANCSMDDEVVERGFASGGGYLATTLVRF
3D structure
PDB2qbu Elucidation of substrate specificity in the cobalamin (vitamin B12) biosynthetic methyltransferases. Structure and function of the C20 methyltransferase (CbiL) from Methanothermobacter thermautotrophicus.
ChainB
Resolution2.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 SAH B P12 L102 G103 D104 I107 Y108 T132 S133 M175 K176 C203 Y220 L221 A222 T223 P12 L102 G103 D104 I107 Y108 T132 S133 M175 K176 C203 Y220 L221 A222 T223 MOAD: Kd=0.645uM
PDBbind-CN: -logKd/Ki=6.19,Kd=0.645uM
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0030788 precorrin-2 C20-methyltransferase activity
Biological Process
GO:0009236 cobalamin biosynthetic process
GO:0032259 methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:2qbu, PDBe:2qbu, PDBj:2qbu
PDBsum2qbu
PubMed17567575
UniProtO27402

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