1NUQ
CRYSTAL STRUCTURE OF HUMAN CYTOSOLIC NMN/NaMN ADENYLYLTRANSFERASE COMPLEXED WITH NaAD
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 | 0004515 | molecular_function | nicotinate-nucleotide adenylyltransferase activity |
| A | 0005524 | molecular_function | ATP binding |
| 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 | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| 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 |
| A | 0070566 | molecular_function | adenylyltransferase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000309 | molecular_function | nicotinamide-nucleotide adenylyltransferase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004515 | molecular_function | nicotinate-nucleotide adenylyltransferase activity |
| B | 0005524 | molecular_function | ATP binding |
| 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 | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| 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 |
| B | 0070566 | molecular_function | adenylyltransferase activity |
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 | HOH694 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | LYS56 |
| A | ALA202 |
| A | THR203 |
| A | HOH645 |
| B | LYS140 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NXX A 401 |
| Chain | Residue |
| A | CYS12 |
| A | GLY13 |
| A | SER14 |
| A | PHE15 |
| A | MET21 |
| A | HIS22 |
| A | TYR53 |
| A | TRP90 |
| A | GLU92 |
| A | THR93 |
| A | CYS134 |
| A | GLY135 |
| A | ASP137 |
| A | VAL138 |
| A | LEU147 |
| A | TRP148 |
| A | ARG167 |
| A | ASN198 |
| A | HOH512 |
| A | HOH519 |
| A | HOH534 |
| A | HOH549 |
| A | HOH573 |
| A | HOH589 |
| A | HOH692 |
| A | HOH745 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 303 |
| Chain | Residue |
| B | LYS95 |
| B | ARG98 |
| B | HIS152 |
| B | HOH774 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 304 |
| Chain | Residue |
| A | LYS140 |
| B | SER201 |
| B | ALA202 |
| B | THR203 |
| B | HOH726 |
| site_id | AC6 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NXX B 402 |
| Chain | Residue |
| B | CYS12 |
| B | GLY13 |
| B | SER14 |
| B | PHE15 |
| B | MET21 |
| B | HIS22 |
| B | VAL49 |
| B | TYR53 |
| B | TRP90 |
| B | GLU92 |
| B | THR93 |
| B | CYS134 |
| B | GLY135 |
| B | ASP137 |
| B | VAL138 |
| B | LEU147 |
| B | TRP148 |
| B | ARG167 |
| B | ASN198 |
| B | GLU199 |
| B | HOH504 |
| B | HOH543 |
| B | HOH563 |
| B | HOH572 |
| B | HOH583 |
| B | HOH614 |
| B | HOH674 |
| B | HOH726 |
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 |
