Structure of PDB 3c9t Chain B

Receptor sequence

>3c9tB (length=309) Species: 63363 (Aquifex aeolicus)

SFTMRLKELGEFGLIDLIKKTLESKVIGDDTAPVEYCSKKLLLTTDVLNE
GVHFLRSYIPEAVGWKAISVNVSDVIANGGLPKWALISLNLPEDLEVSYV
ERFYIGVKRACEFYKCEVVGGNISKSEKIGISVFLVGETERFVGRDGARL
GDSVFVSGTLGDSRAGLELLLMEKEEYEPFELALIQRHLRPTARIDYVKH
IQKYANASMDISDGLVADANHLAQRSGVKIEILSEKLPLSNELKMYCEKY
GKNPIEYALFGGEDYQLLFTHPKERWNPFLDMTEIGRVEEGEGVFVDGKK
VEPKGWKHF

3D structure

• PDB: 3c9t Structural studies of thiamin monophosphate kinase in complex with substrates and products.
• Chain: B
• Resolution: 2.6 Å

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	ACP	B	I12 I24 D26 D27 D71 R142 S209 H218	I15 I27 D29 D30 D74 R145 S212 H221
BS02	MG	B	D27 D71 D207	D30 D74 D210
BS03	MG	B	D43 D71	D46 D74
BS04	MG	B	D210 D215 H218	D213 D218 H221
BS05	ACP	B	I84 Y101 G117 G118 N119 I120	I87 Y104 G120 G121 N122 I123
BS06	TPS	B	V49 H50 L164 H185 E260 W303 H305	V52 H53 L167 H188 E263 W306 H308

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

External links

• PDB: RCSB:3c9t, PDBe:3c9t, PDBj:3c9t
• PDBsum: 3c9t
• PubMed: 18311927
• UniProt: O67883|THIL_AQUAE Thiamine-monophosphate kinase (Gene Name=thiL)