Structure of PDB 1m3u Chain I

Receptor sequence
>1m3uI (length=262) Species: 562 (Escherichia coli) [Search protein sequence]
PTTISLLQKYKQEKKRFATITAYDYSFAKLFADEGLNVMLVGDSLGMTVQ
GHDSTLPVTVADIAYHTAAVRRGAPNCLLLADLPFMAYATPEQAFENAAT
VMRAGANMVKIEGGEWLVETVQMLTERAVPVCGHLGLTPQSVNIFGGYKV
QGRGDEAGDQLLSDALALEAAGAQLLVLECVPVELAKRITEALAIPVIGI
GAGNVTDGQILVMHDAFGITGGHIPKFAKNFLAETGDIRAAVRQYMAEVE
SGVYPGEEHSFH
3D structure
PDB1m3u Structure of E. coli Ketopantoate Hydroxymethyl Transferase Complexed with Ketopantoate and Mg(2+), Solved by Locating 160 Selenomethionine Sites.
ChainI
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.1.2.11: 3-methyl-2-oxobutanoate hydroxymethyltransferase.
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 I D45 D84 D43 D82
BS02 KPL I L42 G44 D45 S46 K112 H136 E181 I212 L40 G42 D43 S44 K110 H134 E179 I210
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0003864 3-methyl-2-oxobutanoate hydroxymethyltransferase activity
GO:0016740 transferase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0015940 pantothenate biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane

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Molecular Function

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Cellular Component
External links
PDB RCSB:1m3u, PDBe:1m3u, PDBj:1m3u
PDBsum1m3u
PubMed12906829
UniProtP31057|PANB_ECOLI 3-methyl-2-oxobutanoate hydroxymethyltransferase (Gene Name=panB)

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