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6UPE

Structure of trehalose-6-phosphate phosphatase from Salmonella typhimurium inhibited by 4-n-octylphenyl alpha-D-glucopyranoside-6-sulfate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004805molecular_functiontrehalose-phosphatase activity
A0005992biological_processtrehalose biosynthetic process
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004805molecular_functiontrehalose-phosphatase activity
B0005992biological_processtrehalose biosynthetic process
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue MG A 301
ChainResidue
AASP20
AASP22
AASP198
AASP199
AASP202
AOGS302
AHOH466

site_idAC2
Number of Residues21
Detailsbinding site for residue OGS A 302
ChainResidue
AASP22
AILE28
ALYS29
APRO30
APRO32
ASER60
AGLY61
AGLU123
ALYS125
AHIS132
AARG134
ALYS163
AVAL165
AGLU167
ALYS175
AMG301
AHOH423
AHOH466
AHOH469
AASP20
ALEU21

site_idAC3
Number of Residues6
Detailsbinding site for residue MG B 301
ChainResidue
BASP20
BASP22
BASP198
BASP199
BASP202
BOGS302

site_idAC4
Number of Residues17
Detailsbinding site for residue OGS B 302
ChainResidue
BASP20
BLEU21
BASP22
BILE28
BSER60
BGLY61
BARG62
BGLU123
BLYS125
BHIS132
BARG134
BLYS163
BCYS164
BVAL165
BGLU167
BLYS175
BMG301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AASP20
BASP20

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP20
AASP22
AASP198
BASP20
BASP22
BASP198

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PDB entries from 2024-07-24

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