1H1Z
The structure of the cytosolic D-ribulose-5-phosphate 3-epimerase from rice complexed with sulfate and zinc
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004750 | molecular_function | D-ribulose-phosphate 3-epimerase activity |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0005737 | cellular_component | cytoplasm |
| 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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A1224 |
| Chain | Residue |
| A | HIS36 |
| A | ASP38 |
| A | HIS69 |
| A | ASP178 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A1225 |
| Chain | Residue |
| A | GLY152 |
| A | GLY180 |
| A | GLY200 |
| A | SER201 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B1224 |
| Chain | Residue |
| B | ASP38 |
| B | HIS69 |
| B | ASP178 |
| B | HIS36 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B1225 |
| Chain | Residue |
| B | GLY152 |
| B | GLY180 |
| B | GLY200 |
| B | SER201 |
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. LHMDImDghFVpNlT |
| Chain | Residue | Details |
| A | LEU35-THR49 |
| site_id | PS01086 |
| Number of Residues | 23 |
| Details | RIBUL_P_3_EPIMER_2 Ribulose-phosphate 3-epimerase family signature 2. VlVMTVePgfgGQkFmpemmeKV |
| Chain | Residue | Details |
| A | VAL141-VAL163 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P32719","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P32719","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P32719","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12547196","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1H1Z","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rpx |
| Chain | Residue | Details |
| A | ASP38 | |
| A | HIS69 | |
| A | ASP178 | |
| A | HIS36 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rpx |
| Chain | Residue | Details |
| B | ASP38 | |
| B | HIS69 | |
| B | ASP178 | |
| B | HIS36 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1rpx |
| Chain | Residue | Details |
| A | ARG120 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1rpx |
| Chain | Residue | Details |
| B | ARG120 |
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 270 |
| Chain | Residue | Details |
| A | SER11 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| A | HIS36 | metal ligand |
| A | ASP38 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| A | MET40 | electrostatic stabiliser |
| A | HIS69 | metal ligand |
| A | MET71 | electrostatic stabiliser |
| A | MET144 | electrostatic stabiliser |
| A | ASP178 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 270 |
| Chain | Residue | Details |
| B | SER11 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| B | HIS36 | metal ligand |
| B | ASP38 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| B | MET40 | electrostatic stabiliser |
| B | HIS69 | metal ligand |
| B | MET71 | electrostatic stabiliser |
| B | MET144 | electrostatic stabiliser |
| B | ASP178 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
