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1EKK

CRYSTAL STRUCTURE OF HYDROXYETHYLTHIAZOLE KINASE IN THE R3 FORM WITH HYDROXYETHYLTHIAZOLE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004417molecular_functionhydroxyethylthiazole kinase activity
A0005524molecular_functionATP binding
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
B0004417molecular_functionhydroxyethylthiazole kinase activity
B0005524molecular_functionATP binding
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 Residues5
DetailsBINDING SITE FOR RESIDUE TZE A 273
ChainResidue
APRO43
AMET45
AGLY67
ATHR194
ACSD198

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE TZE B 273
ChainResidue
BPRO43
BMET45
BGLY67
BCSD198

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO2 A 301
ChainResidue
AASN26
AASN26
AASN26
AHOH380

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO2 B 302
ChainResidue
BASN26
BASN26
BASN26
BHOH357
BHOH398

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00228","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10891066","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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