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1TO9

Crystal structure of THI-4 protein from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0006725biological_processobsolete cellular aromatic compound metabolic process
A0006772biological_processthiamine metabolic process
A0006790biological_processsulfur compound metabolic process
A0009228biological_processthiamine biosynthetic process
A0009229biological_processthiamine diphosphate biosynthetic process
A0016787molecular_functionhydrolase activity
A0044281biological_processsmall molecule metabolic process
A0050334molecular_functionthiaminase activity
A1901360biological_processorganic cyclic compound metabolic process
B0005829cellular_componentcytosol
B0006725biological_processobsolete cellular aromatic compound metabolic process
B0006772biological_processthiamine metabolic process
B0006790biological_processsulfur compound metabolic process
B0009228biological_processthiamine biosynthetic process
B0009229biological_processthiamine diphosphate biosynthetic process
B0016787molecular_functionhydrolase activity
B0044281biological_processsmall molecule metabolic process
B0050334molecular_functionthiaminase activity
B1901360biological_processorganic cyclic compound metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE HMH A 301
ChainResidue
AASP44
ATYR47
AALA81
ALEU85
ACYS135
ATYR139
ATYR163
AGLU205

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HMH B 302
ChainResidue
BTYR47
BCYS135
BTYR139
BTYR163
BGLU205
BASP44

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000303|PubMed:18054064
ChainResidueDetails
BCYS135

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000303|PubMed:18054064
ChainResidueDetails
BGLU205

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15709744, ECO:0000269|Ref.5
ChainResidueDetails
BASP44
BTYR139
BTYR163

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Increases nucleophilicity of active site Cys => ECO:0000303|PubMed:18054064
ChainResidueDetails
BTYR47

221051

PDB entries from 2024-06-12

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