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1VQV

Crystal Structure of Thiamine Monophosphate Kinase (thil) from Aquifex Aeolicus

Replaces:  1YAW
Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0005524molecular_functionATP binding
A0009030molecular_functionthiamine-phosphate kinase activity
A0009228biological_processthiamine biosynthetic process
A0009229biological_processthiamine diphosphate biosynthetic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0005524molecular_functionATP binding
B0009030molecular_functionthiamine-phosphate kinase activity
B0009228biological_processthiamine biosynthetic process
B0009229biological_processthiamine diphosphate biosynthetic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 1001
ChainResidue
AARG184
AASN238
AGLU239
BSER95

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 1002
ChainResidue
AARG187
BTRP273
AILE56
AGLU58
AALA59
ATRP62
AARG106

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 1003
ChainResidue
ASER95
BSER237
BASN238
BGLU239

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 1004
ChainResidue
ATRP273
BILE56
BGLU58
BALA59
BTRP62
BARG106
BARG187

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18311927","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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