3L0G
Crystal structure of Nicotinate-nucleotide pyrophosphorylase from Ehrlichia chaffeensis at 2.05A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009435 | biological_process | NAD+ biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016763 | molecular_function | pentosyltransferase activity |
| A | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| A | 0034213 | biological_process | quinolinate catabolic process |
| B | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009435 | biological_process | NAD+ biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016763 | molecular_function | pentosyltransferase activity |
| B | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| B | 0034213 | biological_process | quinolinate catabolic process |
| C | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009435 | biological_process | NAD+ biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0016763 | molecular_function | pentosyltransferase activity |
| C | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| C | 0034213 | biological_process | quinolinate catabolic process |
| D | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009435 | biological_process | NAD+ biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0016763 | molecular_function | pentosyltransferase activity |
| D | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| D | 0034213 | biological_process | quinolinate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 300 |
| Chain | Residue |
| A | SER128 |
| A | THR129 |
| A | TYR152 |
| A | LEU211 |
| A | GLU234 |
| A | HOH293 |
| A | FMT301 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 300 |
| Chain | Residue |
| B | TYR152 |
| B | GLU234 |
| B | SER256 |
| B | FMT301 |
| B | HOH323 |
| B | SER128 |
| B | THR129 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO C 300 |
| Chain | Residue |
| C | ARG127 |
| C | SER128 |
| C | THR129 |
| C | TYR152 |
| C | LEU211 |
| C | GLU234 |
| C | SER256 |
| C | HOH290 |
| C | FMT301 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 300 |
| Chain | Residue |
| D | ARG127 |
| D | SER128 |
| D | THR129 |
| D | TYR152 |
| D | LEU211 |
| D | GLU234 |
| D | FMT301 |
| D | HOH303 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 301 |
| Chain | Residue |
| A | ARG130 |
| A | ARG153 |
| A | LYS163 |
| A | EDO300 |
| A | HOH304 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT B 301 |
| Chain | Residue |
| B | ARG130 |
| B | ARG153 |
| B | LEU161 |
| B | LYS163 |
| B | HOH293 |
| B | EDO300 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT C 301 |
| Chain | Residue |
| C | ARG130 |
| C | ARG153 |
| C | LEU161 |
| C | LYS163 |
| C | EDO300 |
| C | HOH347 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT D 301 |
| Chain | Residue |
| D | ARG130 |
| D | ARG153 |
| D | LYS163 |
| D | EDO300 |
| D | HOH862 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qpr |
| Chain | Residue | Details |
| A | GLU192 | |
| A | LYS131 | |
| A | ASP213 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qpr |
| Chain | Residue | Details |
| B | GLU192 | |
| B | LYS131 | |
| B | ASP213 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qpr |
| Chain | Residue | Details |
| C | GLU192 | |
| C | LYS131 | |
| C | ASP213 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qpr |
| Chain | Residue | Details |
| D | GLU192 | |
| D | LYS131 | |
| D | ASP213 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qpr |
| Chain | Residue | Details |
| A | ARG96 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qpr |
| Chain | Residue | Details |
| B | ARG96 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qpr |
| Chain | Residue | Details |
| C | ARG96 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qpr |
| Chain | Residue | Details |
| D | ARG96 |
