1OMO
alanine dehydrogenase dimer w/bound NAD (archaeal)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000286 | molecular_function | alanine dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006522 | biological_process | alanine metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000286 | molecular_function | alanine dehydrogenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006522 | biological_process | alanine metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 900 |
| Chain | Residue |
| A | GLY217 |
| A | ALA218 |
| A | GLU225 |
| A | GLU249 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 901 |
| Chain | Residue |
| B | ALA215 |
| B | GLY217 |
| B | ALA218 |
| B | GLU225 |
| B | GLU249 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAD A 400 |
| Chain | Residue |
| A | ARG108 |
| A | THR109 |
| A | GLY134 |
| A | THR135 |
| A | GLN136 |
| A | TYR156 |
| A | ASP157 |
| A | VAL158 |
| A | ARG159 |
| A | THR195 |
| A | PRO196 |
| A | VAL201 |
| A | ILE216 |
| A | GLY217 |
| A | ASP219 |
| A | LYS223 |
| A | SER290 |
| A | THR291 |
| A | GLY292 |
| A | HOH579 |
| A | HOH658 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD B 401 |
| Chain | Residue |
| B | ARG108 |
| B | THR109 |
| B | GLY132 |
| B | GLY134 |
| B | THR135 |
| B | GLN136 |
| B | TYR156 |
| B | ASP157 |
| B | VAL158 |
| B | ARG159 |
| B | THR194 |
| B | THR195 |
| B | PRO196 |
| B | VAL201 |
| B | ILE216 |
| B | GLY217 |
| B | ASP219 |
| B | LYS223 |
| B | SER290 |
| B | THR291 |
| B | GLY292 |
| B | HOH670 |
| B | HOH684 |
| B | HOH692 |
| B | HOH760 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15313611 |
| Chain | Residue | Details |
| A | LYS65 | |
| B | LYS65 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00935, ECO:0000269|PubMed:15313611 |
| Chain | Residue | Details |
| A | ARG108 | |
| B | GLY217 | |
| B | LYS223 | |
| B | SER290 | |
| A | THR135 | |
| A | ASP157 | |
| A | GLY217 | |
| A | LYS223 | |
| A | SER290 | |
| B | ARG108 | |
| B | THR135 | |
| B | ASP157 |
