1U9Z
Crystal Structure of Phosphoribosyl Diphosphate Synthase Complexed with AMP and Ribose 5-Phosphate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0002189 | cellular_component | ribose phosphate diphosphokinase complex |
A | 0004749 | molecular_function | ribose phosphate diphosphokinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006015 | biological_process | 5-phosphoribose 1-diphosphate biosynthetic process |
A | 0006164 | biological_process | purine nucleotide biosynthetic process |
A | 0009156 | biological_process | ribonucleoside monophosphate biosynthetic process |
A | 0009165 | biological_process | nucleotide biosynthetic process |
A | 0016301 | molecular_function | kinase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0002189 | cellular_component | ribose phosphate diphosphokinase complex |
B | 0004749 | molecular_function | ribose phosphate diphosphokinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006015 | biological_process | 5-phosphoribose 1-diphosphate biosynthetic process |
B | 0006164 | biological_process | purine nucleotide biosynthetic process |
B | 0009156 | biological_process | ribonucleoside monophosphate biosynthetic process |
B | 0009165 | biological_process | nucleotide biosynthetic process |
B | 0016301 | molecular_function | kinase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0002189 | cellular_component | ribose phosphate diphosphokinase complex |
C | 0004749 | molecular_function | ribose phosphate diphosphokinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006015 | biological_process | 5-phosphoribose 1-diphosphate biosynthetic process |
C | 0006164 | biological_process | purine nucleotide biosynthetic process |
C | 0009156 | biological_process | ribonucleoside monophosphate biosynthetic process |
C | 0009165 | biological_process | nucleotide biosynthetic process |
C | 0016301 | molecular_function | kinase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0002189 | cellular_component | ribose phosphate diphosphokinase complex |
D | 0004749 | molecular_function | ribose phosphate diphosphokinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0006015 | biological_process | 5-phosphoribose 1-diphosphate biosynthetic process |
D | 0006164 | biological_process | purine nucleotide biosynthetic process |
D | 0009156 | biological_process | ribonucleoside monophosphate biosynthetic process |
D | 0009165 | biological_process | nucleotide biosynthetic process |
D | 0016301 | molecular_function | kinase activity |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE R5P A 5301 |
Chain | Residue |
A | ASP163 |
A | HOH5445 |
A | ASP212 |
A | ILE214 |
A | ILE215 |
A | SER216 |
A | THR217 |
A | GLY218 |
A | GLY219 |
A | THR220 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE R5P B 6301 |
Chain | Residue |
B | ASP163 |
B | ASP212 |
B | ILE214 |
B | ILE215 |
B | SER216 |
B | THR217 |
B | GLY218 |
B | GLY219 |
B | THR220 |
B | HOH6445 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE R5P C 7301 |
Chain | Residue |
C | ASP163 |
C | ASP212 |
C | ILE214 |
C | ILE215 |
C | SER216 |
C | THR217 |
C | GLY218 |
C | GLY219 |
C | THR220 |
C | HOH7445 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE R5P D 8301 |
Chain | Residue |
D | ASP163 |
D | ASP212 |
D | ILE214 |
D | SER216 |
D | THR217 |
D | GLY218 |
D | GLY219 |
D | THR220 |
D | HOH8445 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE AMP B 5302 |
Chain | Residue |
A | ARG92 |
A | GLN93 |
A | ASP94 |
A | PHE97 |
A | HIS125 |
B | PHE32 |
B | ASP34 |
B | GLU36 |
B | HOH5424 |
B | HOH5437 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE AMP B 6302 |
Chain | Residue |
A | PHE32 |
A | ASP34 |
A | GLU36 |
B | ARG92 |
B | GLN93 |
B | ASP94 |
B | PHE97 |
B | HIS125 |
B | HOH6424 |
B | HOH6437 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE AMP D 7302 |
Chain | Residue |
C | ARG92 |
C | GLN93 |
C | PHE97 |
C | HIS125 |
D | PHE32 |
D | ASP34 |
D | GLU36 |
D | HOH7424 |
D | HOH7437 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE AMP C 8302 |
Chain | Residue |
C | PHE32 |
C | ASP34 |
C | GLU36 |
C | HOH8424 |
C | HOH8437 |
D | ARG92 |
D | GLN93 |
D | PHE97 |
D | HIS125 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00583 |
Chain | Residue | Details |
A | LYS186 | |
B | LYS186 | |
C | LYS186 | |
D | LYS186 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:16288921, ECO:0007744|PDB:1U9Z |
Chain | Residue | Details |
B | ASP212 | |
B | SER216 | |
C | ASP34 | |
C | ASP212 | |
C | SER216 | |
D | ASP34 | |
D | ASP212 | |
D | SER216 | |
A | ASP34 | |
A | ASP212 | |
A | SER216 | |
B | ASP34 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000305|PubMed:16288921, ECO:0007744|PDB:1U9Z |
Chain | Residue | Details |
A | ARG92 | |
B | ARG92 | |
C | ARG92 | |
D | ARG92 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583 |
Chain | Residue | Details |
B | ASP163 | |
B | ARG188 | |
C | HIS125 | |
C | ASP163 | |
C | ARG188 | |
D | HIS125 | |
D | ASP163 | |
D | ARG188 | |
A | HIS125 | |
A | ASP163 | |
A | ARG188 | |
B | HIS125 |