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3NL6

The Crystal Structure of Candida glabrata THI6, a Bifunctional Enzyme involved in Thiamin Biosyhthesis of Eukaryotes

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004417molecular_functionhydroxyethylthiazole kinase activity
A0004789molecular_functionthiamine-phosphate diphosphorylase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009228biological_processthiamine biosynthetic process
A0009229biological_processthiamine diphosphate biosynthetic process
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004417molecular_functionhydroxyethylthiazole kinase activity
B0004789molecular_functionthiamine-phosphate diphosphorylase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009228biological_processthiamine biosynthetic process
B0009229biological_processthiamine diphosphate biosynthetic process
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0004417molecular_functionhydroxyethylthiazole kinase activity
C0004789molecular_functionthiamine-phosphate diphosphorylase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0009228biological_processthiamine biosynthetic process
C0009229biological_processthiamine diphosphate biosynthetic process
C0016740molecular_functiontransferase activity
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 541
ChainResidue
AACP799

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 541
ChainResidue
CASP340
CVAL342
CACP899

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG B 541
ChainResidue
BACP999

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE TPS A 2001
ChainResidue
AHIS90
ASER114
ATHR139
ATHR143
ATHR145
AILE179
AGLY181
AVAL209
ASER210
ATYR13
AGLN43
AARG45
AASN75

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TPS C 2002
ChainResidue
CTYR13
CGLN43
CARG45
CASN75
CHIS90
CSER114
CTHR143
CTHR145
CILE179
CGLY181
CSER210

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TPS B 2006
ChainResidue
BTYR13
BGLN43
BARG45
BHIS90
BSER114
BTHR143
BTHR145
BILE179
BGLY181
BVAL209
BSER210

site_idAC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ACP A 799
ChainResidue
AASN369
ATHR416
AGLY417
AGLU418
AASP420
AGLY453
AILE455
AMET458
AALA463
ASER464
AGLY465
ACYS466
ALEU468
ATYR496
ALYS497
AMG541

site_idAC8
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ACP C 899
ChainResidue
CASN369
CTHR416
CGLY417
CGLU418
CASP420
CGLY453
CILE455
CMET458
CALA463
CGLY465
CCYS466
CLEU468
CLYS497
CMG541

site_idAC9
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ACP B 999
ChainResidue
BASN369
BTHR416
BGLY417
BGLU418
BASP420
BILE455
BMET458
BALA463
BGLY465
BCYS466
BLEU468
BTYR496
BLYS497
BMG541

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PDB entries from 2024-08-28

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