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5IBX

1.65 Angstrom Crystal Structure of Triosephosphate Isomerase (TIM) from Streptococcus pneumoniae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0019563biological_processglycerol catabolic process
A0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
B0004807molecular_functiontriose-phosphate isomerase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0019563biological_processglycerol catabolic process
B0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
C0004807molecular_functiontriose-phosphate isomerase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006094biological_processgluconeogenesis
C0006096biological_processglycolytic process
C0016853molecular_functionisomerase activity
C0019563biological_processglycerol catabolic process
C0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
D0004807molecular_functiontriose-phosphate isomerase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006094biological_processgluconeogenesis
D0006096biological_processglycolytic process
D0016853molecular_functionisomerase activity
D0019563biological_processglycerol catabolic process
D0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
E0004807molecular_functiontriose-phosphate isomerase activity
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006094biological_processgluconeogenesis
E0006096biological_processglycolytic process
E0016853molecular_functionisomerase activity
E0019563biological_processglycerol catabolic process
E0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
F0004807molecular_functiontriose-phosphate isomerase activity
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006094biological_processgluconeogenesis
F0006096biological_processglycolytic process
F0016853molecular_functionisomerase activity
F0019563biological_processglycerol catabolic process
F0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
G0004807molecular_functiontriose-phosphate isomerase activity
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0006094biological_processgluconeogenesis
G0006096biological_processglycolytic process
G0016853molecular_functionisomerase activity
G0019563biological_processglycerol catabolic process
G0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
H0004807molecular_functiontriose-phosphate isomerase activity
H0005737cellular_componentcytoplasm
H0005829cellular_componentcytosol
H0006094biological_processgluconeogenesis
H0006096biological_processglycolytic process
H0016853molecular_functionisomerase activity
H0019563biological_processglycerol catabolic process
H0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue NA A 301
ChainResidue
AMET224
ACME226
AVAL229
AHOH453
AHOH606
AHOH618

site_idAC2
Number of Residues6
Detailsbinding site for residue NA B 301
ChainResidue
BHOH445
BHOH637
BHOH645
BMET224
BCME226
BVAL229

site_idAC3
Number of Residues6
Detailsbinding site for residue NA B 302
ChainResidue
BASP198
BHOH629
BHOH659
CHOH511
CHOH577
CHOH599

site_idAC4
Number of Residues6
Detailsbinding site for residue NA C 301
ChainResidue
CMET224
CCYS226
CVAL229
CHOH509
CHOH595
CHOH619

site_idAC5
Number of Residues6
Detailsbinding site for residue NA C 302
ChainResidue
CGLY88
CHOH469
CHOH524
CHOH652
CHOH660
CHOH684

site_idAC6
Number of Residues6
Detailsbinding site for residue NA C 303
ChainResidue
CALA172
CLYS177
CHOH608
CHOH615
EALA197
EHOH415

site_idAC7
Number of Residues6
Detailsbinding site for residue NA C 304
ChainResidue
CHOH498
CHOH540
CHOH550
CHOH622
CHOH653
CHOH718

site_idAC8
Number of Residues6
Detailsbinding site for residue NA D 301
ChainResidue
DMET224
DCME226
DVAL229
DHOH496
DHOH622
DHOH624

site_idAC9
Number of Residues6
Detailsbinding site for residue NA E 301
ChainResidue
EMET224
ECME226
EVAL229
EHOH434
EHOH616
EHOH618

site_idAD1
Number of Residues6
Detailsbinding site for residue NA F 301
ChainResidue
FMET224
FCYS226
FVAL229
FHOH410
FHOH618
FHOH624

site_idAD2
Number of Residues6
Detailsbinding site for residue NA F 302
ChainResidue
FGLY88
FHOH505
FHOH575
FHOH648
FHOH649
FHOH690

site_idAD3
Number of Residues5
Detailsbinding site for residue NA G 301
ChainResidue
GMET224
GCYS226
GVAL229
GHOH439
GHOH557

site_idAD4
Number of Residues6
Detailsbinding site for residue NA H 301
ChainResidue
HMET224
HCME226
HVAL229
HHOH533
HHOH594
HHOH610

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPIWAIGTG
ChainResidueDetails
AALA166-GLY176
CALA166-GLY176

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Electrophile => ECO:0000255|HAMAP-Rule:MF_00147
ChainResidueDetails
CHIS96
FHIS96
GHIS96
EHIS96
HHIS96

site_idSWS_FT_FI2
Number of Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00147
ChainResidueDetails
CGLU168
FGLU168
GGLU168
EGLU168
HGLU168

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00147
ChainResidueDetails
CASN10
GGLY174
GSER214
GGLY235
EASN10
EGLY174
ESER214
EGLY235
HASN10
HGLY174
HSER214
CGLY174
HGLY235
CSER214
CGLY235
FASN10
FGLY174
FSER214
FGLY235
GASN10

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PDB entries from 2025-06-18

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