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1ESJ

CRYSTAL STRUCTURE OF THIAZOLE KINASE MUTANT (C198S)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004417molecular_functionhydroxyethylthiazole kinase activity
A0005524molecular_functionATP binding
A0009228biological_processthiamine biosynthetic process
A0009229biological_processthiamine diphosphate biosynthetic process
A0016301molecular_functionkinase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004417molecular_functionhydroxyethylthiazole kinase activity
B0005524molecular_functionATP binding
B0009228biological_processthiamine biosynthetic process
B0009229biological_processthiamine diphosphate biosynthetic process
B0016301molecular_functionkinase activity
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0004417molecular_functionhydroxyethylthiazole kinase activity
C0005524molecular_functionATP binding
C0009228biological_processthiamine biosynthetic process
C0009229biological_processthiamine diphosphate biosynthetic process
C0016301molecular_functionkinase activity
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 315
ChainResidue
ATHR194
AGLY195
AALA196
AGLY197
ASER198

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 C 325
ChainResidue
CHOH489
CHOH554
CHOH634
CTHR194
CGLY195
CGLY197
CSER198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00228, ECO:0000269|PubMed:10891066
ChainResidueDetails
AMET45
AGLY195
BMET45
BGLY195
CMET45
CGLY195

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AARG121
ATHR168
BARG121
BTHR168
CARG121
CTHR168

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PDB entries from 2024-07-24

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