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1VQV

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

Replaces:  1YAW
Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005524molecular_functionATP binding
A0009030molecular_functionthiamine-phosphate kinase activity
A0009228biological_processthiamine biosynthetic process
A0009229biological_processthiamine diphosphate biosynthetic process
A0016301molecular_functionkinase activity
A0046872molecular_functionmetal ion 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
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 Residues30
DetailsBINDING: BINDING => ECO:0000269|PubMed:18311927
ChainResidueDetails
ATHR42
AASP43
AHIS50
AASP71
ATYR101
AGLY118
AASN119
AARG142
AASP207
ASER209
AASP210
AGLU260
ATRP303
BASP27
BTHR41
BTHR42
BASP43
BHIS50
BASP71
BTYR101
BGLY118
BASN119
BARG142
BASP207
BSER209
BASP210
BGLU260
BTRP303
AASP27
ATHR41

220472

PDB entries from 2024-05-29

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