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1TE2

Putative Phosphatase Ynic from Escherichia coli K12

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003850molecular_function2-deoxyglucose-6-phosphatase activity
A0004346molecular_functionglucose-6-phosphatase activity
A0005829cellular_componentcytosol
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0046872molecular_functionmetal ion binding
A0050084molecular_functionmannitol-1-phosphatase activity
A0050286molecular_functionsorbitol-6-phosphatase activity
A0050308molecular_functionsugar-phosphatase activity
B0000287molecular_functionmagnesium ion binding
B0003850molecular_function2-deoxyglucose-6-phosphatase activity
B0004346molecular_functionglucose-6-phosphatase activity
B0005829cellular_componentcytosol
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0046872molecular_functionmetal ion binding
B0050084molecular_functionmannitol-1-phosphatase activity
B0050286molecular_functionsorbitol-6-phosphatase activity
B0050308molecular_functionsugar-phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PGA A 711
ChainResidue
AASP13
AHOH720
AMSE14
AASP15
AGLY51
ASER115
AALA116
ALYS148
ACA702
AHOH713

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PGA B 712
ChainResidue
BASP13
BMSE14
BASP15
BGLY51
BSER115
BALA116
BLYS148
BCA704
BHOH716
BHOH860
BHOH924

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 701
ChainResidue
AASP130
AASP133
AHOH738
BASP130
BASP133
BHOH743

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 702
ChainResidue
AASP13
AASP15
AASP173
APGA711
AHOH713
AHOH720
AHOH725

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 703
ChainResidue
BGLU106
BHOH829
BHOH927

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 704
ChainResidue
BASP13
BASP15
BASP173
BPGA712
BHOH716
BHOH740
BHOH924

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q8CHP8
ChainResidueDetails
AASP13
BASP13

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q8CHP8
ChainResidueDetails
AASP15
BASP15

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|Ref.7
ChainResidueDetails
AASP13
AASP15
AASP173
BASP13
BASP15
BASP173

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|Ref.7
ChainResidueDetails
ASER115
ALYS148
BSER115
BLYS148

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lvh
ChainResidueDetails
ASER117
ALYS148

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lvh
ChainResidueDetails
BSER117
BLYS148

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lvh
ChainResidueDetails
ALYS148
ASER115

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lvh
ChainResidueDetails
BLYS148
BSER115

224201

PDB entries from 2024-08-28

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