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 | 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 | 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 | 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 | 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 |