1NUU
CRYSTAL STRUCTURE OF HUMAN CYTOSOLIC NMN/NaMN ADENYLYLTRANSFERASE COMPLEXED WITH NAD
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 | 0009611 | biological_process | response to wounding |
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 | 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 | 0009611 | biological_process | response to wounding |
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 | 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 | HOH719 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 302 |
Chain | Residue |
A | SER201 |
A | ALA202 |
A | THR203 |
A | HOH718 |
B | LYS140 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 303 |
Chain | Residue |
B | LYS95 |
B | ARG98 |
B | LYS149 |
B | HIS152 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 304 |
Chain | Residue |
A | LYS140 |
B | SER201 |
B | ALA202 |
B | THR203 |
B | HOH724 |
site_id | AC5 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD A 401 |
Chain | Residue |
A | CYS12 |
A | GLY13 |
A | SER14 |
A | PHE15 |
A | HIS22 |
A | TYR53 |
A | TRP90 |
A | GLU92 |
A | THR93 |
A | CYS134 |
A | GLY135 |
A | ASP137 |
A | LEU147 |
A | TRP148 |
A | ARG167 |
A | ASN198 |
A | HOH506 |
A | HOH507 |
A | HOH521 |
A | HOH530 |
A | HOH556 |
A | HOH561 |
A | HOH718 |
site_id | AC6 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE NAD B 402 |
Chain | Residue |
B | CYS12 |
B | GLY13 |
B | SER14 |
B | PHE15 |
B | MET21 |
B | HIS22 |
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 | HOH502 |
B | HOH555 |
B | HOH577 |
B | HOH600 |
B | HOH602 |
B | HOH669 |
B | HOH717 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12574164, ECO:0007744|PDB:1NUU |
Chain | Residue | Details |
A | SER14 | |
A | ASN198 | |
B | SER14 | |
B | PHE15 | |
B | TRP90 | |
B | THR93 | |
B | GLY135 | |
B | ASP137 | |
B | LEU147 | |
B | TRP148 | |
B | ARG167 | |
A | PHE15 | |
B | ASN198 | |
A | TRP90 | |
A | THR93 | |
A | GLY135 | |
A | ASP137 | |
A | LEU147 | |
A | TRP148 | |
A | ARG167 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: in other chain => ECO:0000269|PubMed:12574164 |
Chain | Residue | Details |
A | HIS22 | |
A | LYS56 | |
A | THR203 | |
B | HIS22 | |
B | LYS56 | |
B | THR203 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12574164 |
Chain | Residue | Details |
A | LYS140 | |
B | LYS140 |