4TTJ
Crystal structure of double mutant E. Coli purine nucleoside phosphorylase with 6 FMC molecules
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
A | 0006152 | biological_process | purine nucleoside catabolic process |
A | 0006974 | biological_process | DNA damage response |
A | 0009116 | biological_process | nucleoside metabolic process |
A | 0009164 | biological_process | nucleoside catabolic process |
A | 0016020 | cellular_component | membrane |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0016763 | molecular_function | pentosyltransferase activity |
A | 0019686 | biological_process | purine nucleoside interconversion |
A | 0042278 | biological_process | purine nucleoside metabolic process |
A | 0042802 | molecular_function | identical protein binding |
A | 0047975 | molecular_function | guanosine phosphorylase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
B | 0006152 | biological_process | purine nucleoside catabolic process |
B | 0006974 | biological_process | DNA damage response |
B | 0009116 | biological_process | nucleoside metabolic process |
B | 0009164 | biological_process | nucleoside catabolic process |
B | 0016020 | cellular_component | membrane |
B | 0016757 | molecular_function | glycosyltransferase activity |
B | 0016763 | molecular_function | pentosyltransferase activity |
B | 0019686 | biological_process | purine nucleoside interconversion |
B | 0042278 | biological_process | purine nucleoside metabolic process |
B | 0042802 | molecular_function | identical protein binding |
B | 0047975 | molecular_function | guanosine phosphorylase activity |
D | 0003824 | molecular_function | catalytic activity |
D | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006139 | biological_process | nucleobase-containing compound metabolic process |
D | 0006152 | biological_process | purine nucleoside catabolic process |
D | 0006974 | biological_process | DNA damage response |
D | 0009116 | biological_process | nucleoside metabolic process |
D | 0009164 | biological_process | nucleoside catabolic process |
D | 0016020 | cellular_component | membrane |
D | 0016757 | molecular_function | glycosyltransferase activity |
D | 0016763 | molecular_function | pentosyltransferase activity |
D | 0019686 | biological_process | purine nucleoside interconversion |
D | 0042278 | biological_process | purine nucleoside metabolic process |
D | 0042802 | molecular_function | identical protein binding |
D | 0047975 | molecular_function | guanosine phosphorylase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue PO4 A 301 |
Chain | Residue |
A | PRO19 |
A | GLY20 |
A | ARG24 |
A | ARG87 |
A | GLY89 |
A | SER90 |
A | FMC302 |
D | ARG43 |
site_id | AC2 |
Number of Residues | 18 |
Details | binding site for residue FMC A 302 |
Chain | Residue |
A | ARG87 |
A | SER90 |
A | CYS91 |
A | GLY92 |
A | PHE159 |
A | VAL178 |
A | GLU179 |
A | MET180 |
A | GLU181 |
A | SER203 |
A | PO4301 |
A | HOH537 |
A | HOH584 |
A | HOH634 |
A | HOH684 |
D | HIS4 |
D | ARG43 |
A | MET64 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 303 |
Chain | Residue |
A | ASN222 |
A | ASP223 |
A | HOH527 |
A | HOH533 |
A | HOH564 |
A | HOH637 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue PO4 B 301 |
Chain | Residue |
B | GLY20 |
B | ARG43 |
B | ARG87 |
B | GLY89 |
B | SER90 |
B | FMC302 |
B | HOH401 |
B | HOH403 |
site_id | AC5 |
Number of Residues | 17 |
Details | binding site for residue FMC B 302 |
Chain | Residue |
B | HIS4 |
B | ARG43 |
B | MET64 |
B | ARG87 |
B | SER90 |
B | CYS91 |
B | GLY92 |
B | PHE159 |
B | VAL178 |
B | GLU179 |
B | MET180 |
B | GLU181 |
B | ILE206 |
B | PO4301 |
B | HOH434 |
B | HOH559 |
B | HOH584 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 303 |
Chain | Residue |
B | LYS99 |
B | LEU100 |
B | HIS205 |
B | GLU210 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 304 |
Chain | Residue |
B | GLN218 |
B | THR219 |
B | ASN222 |
site_id | AC8 |
Number of Residues | 8 |
Details | binding site for residue PO4 D 301 |
Chain | Residue |
A | ARG43 |
D | GLY20 |
D | ARG87 |
D | GLY89 |
D | SER90 |
D | FMC302 |
D | HOH461 |
D | HOH600 |
site_id | AC9 |
Number of Residues | 15 |
Details | binding site for residue FMC D 302 |
Chain | Residue |
A | HIS4 |
A | ARG43 |
D | MET64 |
D | ARG87 |
D | SER90 |
D | CYS91 |
D | GLY92 |
D | PHE159 |
D | VAL178 |
D | GLU179 |
D | MET180 |
D | GLU181 |
D | PO4301 |
D | HOH569 |
D | HOH679 |
Functional Information from PROSITE/UniProt
site_id | PS01232 |
Number of Residues | 16 |
Details | PNP_UDP_1 Purine and other phosphorylases family 1 signature. GhGMGiPScSIytkEL |
Chain | Residue | Details |
A | GLY61-LEU76 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:30337572 |
Chain | Residue | Details |
A | ALA204 | |
B | ALA204 | |
D | ALA204 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:30337572, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ |
Chain | Residue | Details |
A | HIS4 | |
B | HIS4 | |
D | HIS4 |
site_id | SWS_FT_FI3 |
Number of Residues | 9 |
Details | BINDING: in other chain => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ |
Chain | Residue | Details |
A | GLY20 | |
A | ARG24 | |
A | ARG87 | |
B | GLY20 | |
B | ARG24 | |
B | ARG87 | |
D | GLY20 | |
D | ARG24 | |
D | ARG87 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ |
Chain | Residue | Details |
A | ARG43 | |
B | ARG43 | |
D | ARG43 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | BINDING: in other chain => ECO:0000305|PubMed:30337572, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ |
Chain | Residue | Details |
A | GLU179 | |
A | SER203 | |
B | GLU179 | |
B | SER203 | |
D | GLU179 | |
D | SER203 |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | SITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572 |
Chain | Residue | Details |
A | ALA217 | |
B | ALA217 | |
D | ALA217 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
Chain | Residue | Details |
A | LYS26 | |
B | LYS26 | |
D | LYS26 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 375 |
Chain | Residue | Details |
A | GLY20 | electrostatic stabiliser |
A | ARG24 | electrostatic stabiliser |
A | ARG43 | electrostatic stabiliser |
A | ARG87 | electrostatic stabiliser |
A | SER90 | electrostatic stabiliser |
A | ALA204 | proton shuttle (general acid/base) |
A | ALA217 | enhance reactivity |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 375 |
Chain | Residue | Details |
B | GLY20 | electrostatic stabiliser |
B | ARG24 | electrostatic stabiliser |
B | ARG43 | electrostatic stabiliser |
B | ARG87 | electrostatic stabiliser |
B | SER90 | electrostatic stabiliser |
B | ALA204 | proton shuttle (general acid/base) |
B | ALA217 | enhance reactivity |
site_id | MCSA3 |
Number of Residues | 7 |
Details | M-CSA 375 |
Chain | Residue | Details |
D | GLY20 | electrostatic stabiliser |
D | ARG24 | electrostatic stabiliser |
D | ARG43 | electrostatic stabiliser |
D | ARG87 | electrostatic stabiliser |
D | SER90 | electrostatic stabiliser |
D | ALA204 | proton shuttle (general acid/base) |
D | ALA217 | enhance reactivity |