Structure of PDB 2fea Chain A

Receptor sequence
>2feaA (length=225) Species: 1423 (Bacillus subtilis) [Search protein sequence]
TRKPFIICDFDGTITMNDNIINIMKTFAPPEWMALKDGVLSKTLSIKEGV
GRMFGLLPSSLKEEITSFVLEDAKIREGFREFVAFINEHEIPFYVISGGM
DFFVYPLLEGIVEKDRIYCNHASFDNDYIHIDWPHSCKGTCSNQCGCCKP
SVIHELSEPNQYIIMIGDSVTDVEAAKLSDLCFARDYLLNECREQNLNHL
PYQDFYEIRKEIENVKEVQEWLQNK
3D structure
PDB2fea Crystal structure of MtnX phosphatase from Bacillus subtilis at 2.0 A resolution provides a structural basis for bipartite phosphomonoester hydrolysis of 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate.
ChainA
Resolution2.0 Å
3D
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Enzymatic activity
Enzyme Commision number 3.1.3.87: 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase.
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 D11 D13 D170 D9 D11 D168
BS02 ZN A C139 C143 C147 C150 C137 C141 C145 C148
Gene Ontology
Molecular Function
GO:0008253 5'-nucleotidase activity
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0043716 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity
Biological Process
GO:0009086 methionine biosynthetic process
GO:0019509 L-methionine salvage from methylthioadenosine
GO:0071267 L-methionine salvage
Cellular Component
GO:0005737 cytoplasm

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External links
PDB RCSB:2fea, PDBe:2fea, PDBj:2fea
PDBsum2fea
PubMed17654724
UniProtO31667|MTNX_BACSU 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase (Gene Name=mtnX)

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