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5I3K

Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005737cellular_componentcytoplasm
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0019563biological_processglycerol catabolic process
A0020015cellular_componentglycosome
A0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
B0004807molecular_functiontriose-phosphate isomerase activity
B0005737cellular_componentcytoplasm
B0005777cellular_componentperoxisome
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0019563biological_processglycerol catabolic process
B0020015cellular_componentglycosome
B0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
C0004807molecular_functiontriose-phosphate isomerase activity
C0005737cellular_componentcytoplasm
C0005777cellular_componentperoxisome
C0005829cellular_componentcytosol
C0006094biological_processgluconeogenesis
C0006096biological_processglycolytic process
C0016853molecular_functionisomerase activity
C0019563biological_processglycerol catabolic process
C0020015cellular_componentglycosome
C0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
D0004807molecular_functiontriose-phosphate isomerase activity
D0005737cellular_componentcytoplasm
D0005777cellular_componentperoxisome
D0005829cellular_componentcytosol
D0006094biological_processgluconeogenesis
D0006096biological_processglycolytic process
D0016853molecular_functionisomerase activity
D0019563biological_processglycerol catabolic process
D0020015cellular_componentglycosome
D0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue NA A 301
ChainResidue
AALA160
AHOH429
AHOH469

site_idAC2
Number of Residues2
Detailsbinding site for residue NA A 302
ChainResidue
AHOH473
AHOH497

site_idAC3
Number of Residues11
Detailsbinding site for residue PGA B 301
ChainResidue
BGLY173
BGLY234
BGLY235
BHOH405
BHOH421
BHOH445
BHOH447
BLYS13
BGLU167
BALA171
BILE172

site_idAC4
Number of Residues13
Detailsbinding site for residue PGA C 301
ChainResidue
CLYS13
CGLU167
CALA171
CILE172
CGLY173
CGLY212
CVAL214
CALA232
CGLY234
CGLY235
CHOH421
CHOH426
CHOH448

site_idAC5
Number of Residues2
Detailsbinding site for residue NA C 302
ChainResidue
CPHE74
CHOH479

site_idAC6
Number of Residues10
Detailsbinding site for residue PGA D 301
ChainResidue
DLYS13
DGLU167
DILE172
DGLY173
DGLY212
DALA232
DGLY234
DGLY235
DHOH426
DHOH433

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG
ChainResidueDetails
AALA165-GLY175

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Electrophile
ChainResidueDetails
AHIS95
BHIS95
CHIS95
DHIS95

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLU167
BGLU167
CGLU167
DGLU167

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AASN11
ALYS13
BASN11
BLYS13
CASN11
CLYS13
DASN11
DLYS13

218853

PDB entries from 2024-04-24

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