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4Z0S

F96A Mutant of Plasmodium Falciparum Triosephosphate Isomerase

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 Residues5
Detailsbinding site for residue EDO A 301
ChainResidue
AASN10
ALYS12
AHIS95
ALEU230
AGLY232

site_idAC2
Number of Residues2
Detailsbinding site for residue EDO A 302
ChainResidue
ALYS68
AGLU111

site_idAC3
Number of Residues1
Detailsbinding site for residue EDO A 303
ChainResidue
AASP242

site_idAC4
Number of Residues6
Detailsbinding site for residue EDO B 301
ChainResidue
BTHR214
BALA234
BLYS237
BSER239
BPHE240
BASN213

site_idAC5
Number of Residues1
Detailsbinding site for residue EDO B 302
ChainResidue
BASN233

site_idAC6
Number of Residues3
Detailsbinding site for residue EDO B 303
ChainResidue
ASER45
BSER45
BGLY76

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO B 304
ChainResidue
BASN14
BGLY15
BSER19
BLEU23
BLEU236

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

221051

PDB entries from 2024-06-12

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