2QJO
crystal structure of a bifunctional NMN adenylyltransferase/ADP ribose pyrophosphatase (NadM) complexed with ADPRP and NAD from Synechocystis sp.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000309 | molecular_function | nicotinamide-nucleotide adenylyltransferase activity |
A | 0003824 | molecular_function | catalytic activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0009058 | biological_process | biosynthetic process |
A | 0009435 | biological_process | NAD biosynthetic process |
A | 0016779 | molecular_function | nucleotidyltransferase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
A | 0042802 | molecular_function | identical protein binding |
B | 0000309 | molecular_function | nicotinamide-nucleotide adenylyltransferase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0009058 | biological_process | biosynthetic process |
B | 0009435 | biological_process | NAD biosynthetic process |
B | 0016779 | molecular_function | nucleotidyltransferase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
B | 0042802 | molecular_function | identical protein binding |
C | 0000309 | molecular_function | nicotinamide-nucleotide adenylyltransferase activity |
C | 0003824 | molecular_function | catalytic activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0009058 | biological_process | biosynthetic process |
C | 0009435 | biological_process | NAD biosynthetic process |
C | 0016779 | molecular_function | nucleotidyltransferase activity |
C | 0016787 | molecular_function | hydrolase activity |
C | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
C | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 402 |
Chain | Residue |
A | ARG43 |
A | ARG53 |
A | HOH805 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 403 |
Chain | Residue |
A | LYS4 |
A | LYS31 |
A | ASN104 |
A | HOH731 |
A | HOH794 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 404 |
Chain | Residue |
A | ARG43 |
A | ARG79 |
A | HOH825 |
B | HOH788 |
A | HIS42 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 401 |
Chain | Residue |
A | ASP316 |
B | HIS42 |
B | ARG43 |
B | ARG79 |
site_id | AC5 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE APR A 501 |
Chain | Residue |
A | TYR188 |
A | PHE201 |
A | THR203 |
A | ASP205 |
A | ARG219 |
A | GLY232 |
A | GLY233 |
A | PHE234 |
A | GLU248 |
A | GLU252 |
A | ARG277 |
A | ARG280 |
A | THR283 |
A | GLU326 |
A | HIS328 |
A | HOH767 |
A | HOH769 |
A | HOH799 |
A | HOH818 |
A | HOH819 |
C | TYR197 |
site_id | AC6 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD A 601 |
Chain | Residue |
A | TYR10 |
A | ILE11 |
A | GLY12 |
A | ARG13 |
A | PHE14 |
A | HIS21 |
A | GLY40 |
A | SER41 |
A | ASP80 |
A | TRP81 |
A | ASP85 |
A | TRP88 |
A | HIS111 |
A | TYR118 |
A | TYR119 |
A | GLY132 |
A | HIS133 |
A | TYR134 |
A | PHE137 |
A | HOH710 |
A | HOH717 |
A | HOH774 |
A | HOH810 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE POP A 701 |
Chain | Residue |
A | ARG13 |
A | LYS113 |
A | SER138 |
A | SER139 |
A | THR140 |
A | ARG143 |
site_id | AC8 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE APR B 502 |
Chain | Residue |
B | TYR188 |
B | TYR197 |
B | PHE201 |
B | THR203 |
B | ASP205 |
B | ARG219 |
B | GLY232 |
B | GLY233 |
B | PHE234 |
B | GLU248 |
B | GLU252 |
B | ARG277 |
B | ARG280 |
B | GLU326 |
B | HIS328 |
B | HOH730 |
B | HOH775 |
B | HOH791 |
B | HOH799 |
B | HOH834 |
site_id | AC9 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAD B 602 |
Chain | Residue |
B | TRP88 |
B | HIS111 |
B | LYS113 |
B | TYR118 |
B | TYR119 |
B | GLY132 |
B | HIS133 |
B | TYR134 |
B | PHE137 |
B | HOH734 |
B | HOH741 |
B | HOH745 |
B | TYR10 |
B | ILE11 |
B | GLY12 |
B | ARG13 |
B | PHE14 |
B | HIS18 |
B | HIS21 |
B | GLY40 |
B | SER41 |
B | ASP80 |
B | TRP81 |
B | ASP85 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE POP B 702 |
Chain | Residue |
B | ARG13 |
B | ARG49 |
B | LYS113 |
B | SER138 |
B | SER139 |
B | THR140 |
B | ARG143 |
site_id | BC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE APR C 503 |
Chain | Residue |
A | TYR197 |
C | TYR188 |
C | PHE201 |
C | THR203 |
C | ASP205 |
C | ARG219 |
C | GLY232 |
C | GLY233 |
C | PHE234 |
C | GLU248 |
C | GLU252 |
C | ARG277 |
C | ARG280 |
C | GLU326 |
C | HIS328 |
C | HOH731 |
C | HOH748 |
site_id | BC3 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE NAD C 603 |
Chain | Residue |
C | TYR10 |
C | ILE11 |
C | GLY12 |
C | ARG13 |
C | PHE14 |
C | HIS18 |
C | GLY40 |
C | SER41 |
C | ASP80 |
C | TRP81 |
C | SER84 |
C | ASP85 |
C | TRP88 |
C | GLY110 |
C | HIS111 |
C | TYR118 |
C | TYR119 |
C | HIS133 |
C | TYR134 |
C | PHE137 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE POP C 703 |
Chain | Residue |
C | ARG13 |
C | LYS113 |
C | SER138 |
C | SER139 |
C | THR140 |
C | ARG143 |
Functional Information from PROSITE/UniProt
site_id | PS00893 |
Number of Residues | 22 |
Details | NUDIX_BOX Nudix box signature. GfikqnEtlveGMlRELkEEtR |
Chain | Residue | Details |
A | GLY233-ARG254 |