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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| 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 | 0000166 | molecular_function | nucleotide 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 | 0016740 | molecular_function | transferase activity |
| 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 | 0000166 | molecular_function | nucleotide 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 | 0016740 | molecular_function | transferase activity |
| 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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 182 |
| Details | Region: {"description":"NMN adenylyltransferase"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 63 |
| Details | Motif: {"description":"Nudix box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 136 |
| Details | Domain: {"description":"Nudix hydrolase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
