Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2VFI

Crystal structure of the Plasmodium falciparum triosephosphate isomerase in the loop closed state with 3-phosphoglycerate bound at the active site and interface

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0042802molecular_functionidentical protein binding
B0004807molecular_functiontriose-phosphate isomerase activity
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 3PG A 1249
ChainResidue
AASN10
ALEU230
AGLY232
AASN233
AHOH2163
AHOH2164
AHOH2165
AHOH2167
ALYS12
AHIS95
AALA169
AILE170
AGLY171
AGLY209
AGLY210
ASER211

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 3PG A 1250
ChainResidue
AASN65
ALYS68
AARG98
APHE102
AHIS103
AGLU104
AASP108
ALYS112
AHOH2070
AHOH2168
AHOH2169
AHOH2170
BTYR101
BPHE102
BHIS103
BHOH2182

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 3PG B 1249
ChainResidue
BASN10
BLYS12
BHIS95
BGLU165
BILE170
BGLY171
BSER211
BLEU230
BGLY232
BASN233
BHOH2179
BHOH2180
BHOH2181

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 3PG B 1250
ChainResidue
ATYR101
APHE102
AHIS103
AHOH2170
BASN65
BLYS68
BARG98
BPHE102
BHIS103
BGLU104
BASP108
BLYS112
BHOH2074
BHOH2075
BHOH2096
BHOH2182

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

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon