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5I3H

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
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0020015cellular_componentglycosome
B0004807molecular_functiontriose-phosphate isomerase activity
B0005737cellular_componentcytoplasm
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0020015cellular_componentglycosome
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue K A 301
ChainResidue
AVAL214
AALA236
AHOH447
BHOH498

site_idAC2
Number of Residues4
Detailsbinding site for residue K A 302
ChainResidue
AASN15
BGLY72
BALA73
BHOH561

site_idAC3
Number of Residues15
Detailsbinding site for residue PGA B 301
ChainResidue
BHIS95
BGLU167
BALA171
BALA172
BGLY173
BSER213
BGLY234
BGLY235
BHOH428
BHOH432
BHOH440
BHOH458
BHOH462
BHOH492
BLYS13

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Electrophile
ChainResidueDetails
AHIS95
BHIS95

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLU167
BGLU167

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AASN11
ALYS13
BASN11
BLYS13

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PDB entries from 2024-07-24

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