Structure of PDB 2pup Chain A

Receptor sequence
>2pupA (length=371) Species: 1423 (Bacillus subtilis) [Search protein sequence]
PLYETLNESSAVLAVKLLTCQEIGDGNLNYVFHIYDQDRALIIKQAVPYP
LTIDRARIESSALIRQGEHVPHLVPRVFYSDTEMAVTVMEDLSHLKIARK
GLIEGENYPHLSQHIGEFLGKTLFYSSDYALEPKVKKQLVKQFTNPELCD
ITERLVFTDPFFDHDTNDFEEELRPFVEKLWNNDSVKIEAAKLKKSFLTS
AETLIHGDLHTGSIFASEHETKVIDPEFAFYGPIGFDVGQFIANLFLNAL
SRDGADREPLYEHVNQVWETFEETFSEAWQKDSLDVYANIDGYLTDTLSH
IFEEAIGFAGCELIRRTIGLAHVADLDTIVPFDKRIGRKRLALETGTAFI
EKRSEFKTITDVIELFKLLVK
3D structure
PDB2pup Structures of 5-methylthioribose kinase reveal substrate specificity and unusual mode of nucleotide binding
ChainA
Resolution2.6 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 A D250 E252 D225 E227
BS02 ADP A N44 I59 K61 E115 D116 L117 F240 D250 N29 I42 K44 E90 D91 L92 F215 D225
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2pup, PDBe:2pup, PDBj:2pup
PDBsum2pup
PubMed17522047
UniProtO31663|MTNK_BACSU Methylthioribose kinase (Gene Name=mtnK)

[Back to BioLiP]