3CTL
Crystal structure of D-Allulose 6-Phosphate 3-Epimerase from Escherichia coli K12 complexed with D-glucitol 6-phosphate and magnesium
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 | 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 | 0019316 | biological_process | D-allose catabolic process |
| A | 0034700 | molecular_function | allulose 6-phosphate 3-epimerase activity |
| 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 | 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 | 0019316 | biological_process | D-allose catabolic process |
| B | 0034700 | molecular_function | allulose 6-phosphate 3-epimerase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004750 | molecular_function | D-ribulose-phosphate 3-epimerase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| C | 0019316 | biological_process | D-allose catabolic process |
| C | 0034700 | molecular_function | allulose 6-phosphate 3-epimerase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004750 | molecular_function | D-ribulose-phosphate 3-epimerase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| D | 0019316 | biological_process | D-allose catabolic process |
| D | 0034700 | molecular_function | allulose 6-phosphate 3-epimerase activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0004750 | molecular_function | D-ribulose-phosphate 3-epimerase activity |
| E | 0005829 | cellular_component | cytosol |
| E | 0005975 | biological_process | carbohydrate metabolic process |
| E | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| E | 0016853 | molecular_function | isomerase activity |
| E | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| E | 0019316 | biological_process | D-allose catabolic process |
| E | 0034700 | molecular_function | allulose 6-phosphate 3-epimerase activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0004750 | molecular_function | D-ribulose-phosphate 3-epimerase activity |
| F | 0005829 | cellular_component | cytosol |
| F | 0005975 | biological_process | carbohydrate metabolic process |
| F | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| F | 0016853 | molecular_function | isomerase activity |
| F | 0016857 | molecular_function | racemase and epimerase activity, acting on carbohydrates and derivatives |
| F | 0019316 | biological_process | D-allose catabolic process |
| F | 0034700 | molecular_function | allulose 6-phosphate 3-epimerase activity |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE S6P A 501 |
| Chain | Residue |
| A | SER6 |
| A | ALA142 |
| A | GLY143 |
| A | ASP173 |
| A | GLY174 |
| A | SER175 |
| A | GLY195 |
| A | THR196 |
| A | SER197 |
| A | MET8 |
| A | HIS30 |
| A | ASP32 |
| A | HIS63 |
| A | MET65 |
| A | PRO139 |
| A | GLY140 |
| A | PHE141 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE S6P B 502 |
| Chain | Residue |
| B | SER6 |
| B | MET8 |
| B | HIS30 |
| B | ASP32 |
| B | HIS63 |
| B | MET65 |
| B | GLY140 |
| B | PHE141 |
| B | ALA142 |
| B | GLY143 |
| B | ASP173 |
| B | GLY174 |
| B | SER175 |
| B | GLY195 |
| B | THR196 |
| B | SER197 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE S6P C 503 |
| Chain | Residue |
| C | SER6 |
| C | MET8 |
| C | HIS30 |
| C | ASP32 |
| C | HIS63 |
| C | MET65 |
| C | PRO139 |
| C | GLY140 |
| C | PHE141 |
| C | ALA142 |
| C | GLY143 |
| C | ASP173 |
| C | GLY174 |
| C | SER175 |
| C | GLY195 |
| C | THR196 |
| C | SER197 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE S6P D 504 |
| Chain | Residue |
| D | SER6 |
| D | MET8 |
| D | HIS30 |
| D | ASP32 |
| D | HIS63 |
| D | PRO139 |
| D | GLY140 |
| D | PHE141 |
| D | ALA142 |
| D | GLY143 |
| D | ASP173 |
| D | GLY174 |
| D | SER175 |
| D | GLY195 |
| D | THR196 |
| D | SER197 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE S6P E 505 |
| Chain | Residue |
| E | SER6 |
| E | MET8 |
| E | HIS30 |
| E | ASP32 |
| E | HIS63 |
| E | MET65 |
| E | PRO139 |
| E | GLY140 |
| E | PHE141 |
| E | ALA142 |
| E | GLY143 |
| E | ASP173 |
| E | GLY174 |
| E | SER175 |
| E | GLY195 |
| E | THR196 |
| E | SER197 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE S6P F 506 |
| Chain | Residue |
| F | SER197 |
| F | SER6 |
| F | MET8 |
| F | HIS30 |
| F | ASP32 |
| F | HIS63 |
| F | MET65 |
| F | PRO139 |
| F | GLY140 |
| F | PHE141 |
| F | ALA142 |
| F | GLY143 |
| F | ASP173 |
| F | GLY174 |
| F | SER175 |
| F | GLY195 |
| F | THR196 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 601 |
| Chain | Residue |
| A | HIS30 |
| A | ASP32 |
| A | HIS63 |
| A | ASP173 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 602 |
| Chain | Residue |
| B | HIS30 |
| B | ASP32 |
| B | HIS63 |
| B | ASP173 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 603 |
| Chain | Residue |
| C | HIS30 |
| C | ASP32 |
| C | HIS63 |
| C | ASP173 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 604 |
| Chain | Residue |
| D | HIS30 |
| D | ASP32 |
| D | HIS63 |
| D | ASP173 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG E 605 |
| Chain | Residue |
| E | HIS30 |
| E | ASP32 |
| E | HIS63 |
| E | ASP173 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG F 606 |
| Chain | Residue |
| F | HIS30 |
| F | ASP32 |
| F | HIS63 |
| F | ASP173 |
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. FHIDImDghFVpNlT |
| Chain | Residue | Details |
| A | PHE29-THR43 |
| site_id | PS01086 |
| Number of Residues | 23 |
| Details | RIBUL_P_3_EPIMER_2 Ribulose-phosphate 3-epimerase family signature 2. ItVMTVdPgfaGQpFipemldKL |
| Chain | Residue | Details |
| A | ILE132-LEU154 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02226, ECO:0000269|PubMed:18700786, ECO:0007744|PDB:3CTL |
| Chain | Residue | Details |
| A | ASP32 | |
| B | ASP32 | |
| C | ASP32 | |
| D | ASP32 | |
| E | ASP32 | |
| F | ASP32 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_02226, ECO:0000269|PubMed:18700786, ECO:0007744|PDB:3CTL |
| Chain | Residue | Details |
| A | ASP173 | |
| B | ASP173 | |
| C | ASP173 | |
| D | ASP173 | |
| E | ASP173 | |
| F | ASP173 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02226, ECO:0000269|PubMed:18700786, ECO:0007744|PDB:3CTL |
| Chain | Residue | Details |
| A | SER6 | |
| C | HIS63 | |
| C | GLY140 | |
| C | GLY195 | |
| D | SER6 | |
| D | HIS63 | |
| D | GLY140 | |
| D | GLY195 | |
| E | SER6 | |
| E | HIS63 | |
| E | GLY140 | |
| A | HIS63 | |
| E | GLY195 | |
| F | SER6 | |
| F | HIS63 | |
| F | GLY140 | |
| F | GLY195 | |
| A | GLY140 | |
| A | GLY195 | |
| B | SER6 | |
| B | HIS63 | |
| B | GLY140 | |
| B | GLY195 | |
| C | SER6 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02226, ECO:0000269|PubMed:18700786, ECO:0007744|PDB:3CT7, ECO:0007744|PDB:3CTL |
| Chain | Residue | Details |
| A | HIS30 | |
| D | HIS30 | |
| D | ASP32 | |
| D | ASP173 | |
| E | HIS30 | |
| E | ASP32 | |
| E | ASP173 | |
| F | HIS30 | |
| F | ASP32 | |
| F | ASP173 | |
| A | ASP32 | |
| A | ASP173 | |
| B | HIS30 | |
| B | ASP32 | |
| B | ASP173 | |
| C | HIS30 | |
| C | ASP32 | |
| C | ASP173 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rpx |
| Chain | Residue | Details |
| A | HIS30 | |
| A | ASP32 | |
| A | ASP173 | |
| A | HIS63 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rpx |
| Chain | Residue | Details |
| B | HIS30 | |
| B | ASP32 | |
| B | ASP173 | |
| B | HIS63 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rpx |
| Chain | Residue | Details |
| C | HIS30 | |
| C | ASP32 | |
| C | ASP173 | |
| C | HIS63 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rpx |
| Chain | Residue | Details |
| D | HIS30 | |
| D | ASP32 | |
| D | ASP173 | |
| D | HIS63 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rpx |
| Chain | Residue | Details |
| E | HIS30 | |
| E | ASP32 | |
| E | ASP173 | |
| E | HIS63 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rpx |
| Chain | Residue | Details |
| F | HIS30 | |
| F | ASP32 | |
| F | ASP173 | |
| F | HIS63 |
