1NUR
CRYSTAL STRUCTURE OF HUMAN CYTOSOLIC NMN/NaMN ADENYLYLTRANSFERASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000309 | molecular_function | nicotinamide-nucleotide adenylyltransferase activity |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004515 | molecular_function | nicotinate-nucleotide adenylyltransferase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0009435 | biological_process | NAD+ biosynthetic process |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0030424 | cellular_component | axon |
| A | 0034355 | biological_process | NAD+ biosynthetic process via the salvage pathway |
| A | 0034612 | biological_process | response to tumor necrosis factor |
| A | 0043025 | cellular_component | neuronal cell body |
| B | 0000309 | molecular_function | nicotinamide-nucleotide adenylyltransferase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004515 | molecular_function | nicotinate-nucleotide adenylyltransferase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0009435 | biological_process | NAD+ biosynthetic process |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0030424 | cellular_component | axon |
| B | 0034355 | biological_process | NAD+ biosynthetic process via the salvage pathway |
| B | 0034612 | biological_process | response to tumor necrosis factor |
| B | 0043025 | cellular_component | neuronal cell body |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 301 |
| Chain | Residue |
| A | LYS95 |
| A | ARG98 |
| A | HIS152 |
| A | HOH493 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | HOH415 |
| A | HOH480 |
| A | HOH481 |
| A | HOH634 |
| A | HOH639 |
| A | SER14 |
| A | LYS56 |
| A | ALA202 |
| A | THR203 |
| A | ARG206 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 303 |
| Chain | Residue |
| B | ARG98 |
| B | HIS152 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 304 |
| Chain | Residue |
| A | HOH544 |
| B | SER14 |
| B | ALA202 |
| B | THR203 |
| B | ARG206 |
| B | HOH438 |
| B | HOH440 |
| B | HOH520 |
| B | HOH640 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 305 |
| Chain | Residue |
| A | LYS173 |
| B | LYS193 |
| B | PRO195 |
| B | ARG207 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12574164","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NUU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"12574164","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12574164","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
