1TQX
Crystal Structure of Pfal009167 A Putative D-Ribulose 5-Phosphate 3-Epimerase from P.falciparum
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004750 | molecular_function | D-ribulose-phosphate 3-epimerase activity |
A | 0005829 | cellular_component | cytosol |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0006098 | biological_process | pentose-phosphate shunt |
A | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
A | 0016853 | molecular_function | isomerase activity |
A | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
A | 0046872 | molecular_function | metal ion binding |
B | 0004750 | molecular_function | D-ribulose-phosphate 3-epimerase activity |
B | 0005829 | cellular_component | cytosol |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0006098 | biological_process | pentose-phosphate shunt |
B | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
B | 0016853 | molecular_function | isomerase activity |
B | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 2224 |
Chain | Residue |
A | GLY152 |
A | HOH1232 |
A | GLY153 |
A | GLY181 |
A | GLY201 |
A | THR202 |
A | HOH1001 |
A | HOH1019 |
A | HOH1033 |
A | HOH1039 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SO4 B 3224 |
Chain | Residue |
B | GLY152 |
B | GLY153 |
B | GLY180 |
B | GLY181 |
B | GLY201 |
B | THR202 |
B | HOH1055 |
B | HOH1073 |
B | HOH1087 |
B | HOH1093 |
B | HOH1239 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 900 |
Chain | Residue |
A | HIS36 |
A | ASP38 |
A | HIS70 |
A | ASP179 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 902 |
Chain | Residue |
B | HIS36 |
B | ASP38 |
B | HIS70 |
B | ASP179 |
Functional Information from PROSITE/UniProt
site_id | PS01085 |
Number of Residues | 15 |
Details | RIBUL_P_3_EPIMER_1 Ribulose-phosphate 3-epimerase family signature 1. IHLDVmDmhFVpNlS |
Chain | Residue | Details |
A | ILE35-SER49 |
site_id | PS01086 |
Number of Residues | 23 |
Details | RIBUL_P_3_EPIMER_2 Ribulose-phosphate 3-epimerase family signature 2. VlVMTVePgfgGQsFmhdmmgKV |
Chain | Residue | Details |
A | VAL142-VAL164 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qpr |
Chain | Residue | Details |
A | SER29 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qpr |
Chain | Residue | Details |
B | SER29 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qpr |
Chain | Residue | Details |
A | ASP179 | |
A | ASP38 | |
A | HIS70 | |
A | HIS36 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qpr |
Chain | Residue | Details |
B | ASP179 | |
B | ASP38 | |
B | HIS70 | |
B | HIS36 |