Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3TVL

Complex between the human thiamine triphosphatase and triphosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006091biological_processgeneration of precursor metabolites and energy
A0006772biological_processthiamine metabolic process
A0009229biological_processthiamine diphosphate biosynthetic process
A0016311biological_processdephosphorylation
A0016462molecular_functionpyrophosphatase activity
A0016787molecular_functionhydrolase activity
A0042357biological_processthiamine diphosphate metabolic process
A0046872molecular_functionmetal ion binding
A0050333molecular_functionthiamine triphosphate phosphatase activity
B0000287molecular_functionmagnesium ion binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006091biological_processgeneration of precursor metabolites and energy
B0006772biological_processthiamine metabolic process
B0009229biological_processthiamine diphosphate biosynthetic process
B0016311biological_processdephosphorylation
B0016462molecular_functionpyrophosphatase activity
B0016787molecular_functionhydrolase activity
B0042357biological_processthiamine diphosphate metabolic process
B0046872molecular_functionmetal ion binding
B0050333molecular_functionthiamine triphosphate phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 3PO A 231
ChainResidue
ALYS11
AHOH243
AHOH252
AHOH254
AHOH287
ATYR39
AARG55
AARG57
ALYS65
AARG125
AGLU157
ALYS193
AHOH242

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 232
ChainResidue
ATYR39
ATYR40
ALEU47
AHIS52
ATRP53
ALEU54

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 3PO B 231
ChainResidue
BLYS11
BTYR39
BARG55
BARG57
BLYS65
BGLU81
BARG125
BGLU157
BALA192
BLYS193
BHOH238

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 232
ChainResidue
APHE201
BARG36
BTHR38
BARG56
BGLU58

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO B 233
ChainResidue
BTYR39
BTYR40
BASP41
BLEU47
BMET48
BHIS52
BTRP53
BLEU54
BLEU194

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLU7
AGLU9
AASP145
AGLU159
BGLU7
BGLU9
BASP145
BGLU159

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING:
ChainResidueDetails
ALYS11
BLYS65
BARG125
BGLU157
AARG55
AARG57
ALYS65
AARG125
AGLU157
BLYS11
BARG55
BARG57

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ALYS193
BLYS193

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2
BALA2

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon