Structure of PDB 6mfm Chain A

Receptor sequence
>6mfmA (length=304) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
AEFSIIDQYFNRQSHPDVALGIGDDSALITPPPNQQLVICADTLVAGRHF
PLETSPHAIGWKSVAVNLSDIAAMGAKPHSILLAISLPQVDHEWLEGFSQ
GIYDCCNQFGVALIGGDTTQGPHLTITVTAMGWIETGKAVLRSGAKVGDY
VCVSGQIGDAAYGLQHLGHSLQQRLDYPTPRCKLGEELKGLASSMIDVSD
GLAQDLGHILKASKVGARLILEKLPVDPVLQQIEEQQRWQYALAGGDDYE
LCFTITPQNYEKLLQKQLDVKITMIGQIVEQTKLTFEHLGSDYPLQIHGY
QHFA
3D structure
PDB6mfm Crystal structures of thiamine monophosphate kinase from Acinetobacter baumannii in complex with substrates and products.
ChainA
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.4.16: thiamine-phosphate 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 TPP A D43 R49 H50 F51 P52 L165 S200 D201 D248 Y301 H303 D42 R48 H49 F50 P51 L164 S199 D200 D247 Y300 H302
BS02 MG A D43 D71 D42 D70
BS03 MG A D71 D198 D70 D197
BS04 ADP A I7 F11 I23 G24 D25 L84 G116 G117 D118 T119 I6 F10 I22 G23 D24 L83 G115 G116 D117 T118
BS05 ADP A D43 D71 D42 D70
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0005524 ATP binding
GO:0009030 thiamine-phosphate kinase activity
GO:0016301 kinase activity
GO:0046872 metal ion binding
Biological Process
GO:0009228 thiamine biosynthetic process
GO:0009229 thiamine diphosphate biosynthetic process
GO:0016310 phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:6mfm, PDBe:6mfm, PDBj:6mfm
PDBsum6mfm
PubMed30867460
UniProtA0A0D5YC82

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