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BioLiP

Structure of PDB 2pul Chain B

Receptor sequence
>2pulB (length=369) Species: 1423 (Bacillus subtilis) [Search protein sequence]
PLYETLNESSAVALAVKLGLTCQEIGDGNLNYVFHIYRALIIKQAVPPLT
IDRARIESSALIRQGEHVPHLVPRVFYSDTEMAVTVMEDLSHLKIARKGL
IEGENYPHLSQHIGEFLGKTLFYSSDYALEPKVKKQLVKQFTNPELCDIT
ERLVFTDPFFDHDTNDFEEELRPFVEKLWNNDSVKIEAAKLKKSFLTSAE
TLIHGDLHTGSIFASEHETKVIDPEFAFYGPIGFDVGQFIANLFLNALSR
DGADREPLYEHVNQVWETFEETFSEAWQKDSLDVYANIDGYLTDTLSHIF
EEAIGFAGCELIRRTIGLAHVADLDTIVPFDKRIGRKRLALETGTAFIEK
RSEFKTITDVIELFKLLVK
3D structure
PDB2pul Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding
ChainB
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.1.100: S-methyl-5-thioribose kinase.
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 MG B D250 E252 D223 E225
BS02 ACP B D40 N44 I59 K61 M114 D116 L117 F240 D250 D27 N31 I41 K43 M87 D89 L90 F213 D223
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0046522 S-methyl-5-thioribose kinase activity
Biological Process
GO:0009086 methionine biosynthetic process
GO:0016310 phosphorylation
GO:0019509 L-methionine salvage from methylthioadenosine

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Molecular Function

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Biological Process
External links
PDB RCSB:2pul, PDBe:2pul, PDBj:2pul
PDBsum2pul
PubMed17522047
UniProtO31663|MTNK_BACSU Methylthioribose kinase (Gene Name=mtnK)

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