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1M7P

Plasmodium Falciparum Triosephosphate isomerase (PfTIM) compled to substrate analog glycerol-3-phosphate (G3P).

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0019563biological_processglycerol catabolic process
A0042802molecular_functionidentical protein binding
A0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
B0004807molecular_functiontriose-phosphate isomerase activity
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0019563biological_processglycerol catabolic process
B0042802molecular_functionidentical protein binding
B0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE G3H A 5401
ChainResidue
AASN10
ALYS12
AHIS95
APHE96
ASER211
ALEU230
AGLY232
AASN233
AHOH523

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE G3H B 6401
ChainResidue
BASN10
BLYS12
BHIS95
BLEU230
BGLY232
BASN233
BHOH517

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. VYEPLWAIGTG
ChainResidueDetails
AVAL163-GLY173

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Electrophile => ECO:0000255|PROSITE-ProRule:PRU10127
ChainResidueDetails
AHIS95
BHIS95

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10127
ChainResidueDetails
AGLU165
BGLU165

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12454456, ECO:0000269|PubMed:14563846, ECO:0000269|PubMed:19622869, ECO:0007744|PDB:1M7O, ECO:0007744|PDB:1O5X, ECO:0007744|PDB:2VFI
ChainResidueDetails
AASN10
BASN10

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12403619, ECO:0000269|PubMed:15465054, ECO:0000269|PubMed:19622869, ECO:0007744|PDB:1LYX, ECO:0007744|PDB:1LZO, ECO:0007744|PDB:1WOA, ECO:0007744|PDB:2VFI
ChainResidueDetails
ALYS12
BLYS12

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12403619, ECO:0000269|PubMed:19622869, ECO:0007744|PDB:1LYX, ECO:0007744|PDB:2VFI
ChainResidueDetails
AGLY171
BGLY171

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12454456, ECO:0000269|PubMed:14563846, ECO:0000269|PubMed:15465054, ECO:0000269|PubMed:19622869, ECO:0007744|PDB:1M7O, ECO:0007744|PDB:1O5X, ECO:0007744|PDB:1WOA, ECO:0007744|PDB:2VFI
ChainResidueDetails
ALEU230
BLEU230

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12403619, ECO:0000269|PubMed:12454456, ECO:0000269|PubMed:14563846, ECO:0000269|PubMed:15465054, ECO:0000269|PubMed:19622869, ECO:0000312|PDB:1LZO, ECO:0007744|PDB:1LYX, ECO:0007744|PDB:1M7O, ECO:0007744|PDB:1M7P, ECO:0007744|PDB:1O5X, ECO:0007744|PDB:1WOA, ECO:0007744|PDB:2VFI
ChainResidueDetails
AGLY232
BGLY232

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
AASN10
AHIS95
AGLU165
AGLY171
ALYS12

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
BASN10
BHIS95
BGLU165
BGLY171
BLYS12

229380

PDB entries from 2024-12-25

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