2VHY
Crystal structure of apo L-alanine dehydrogenase from Mycobacterium tuberculosis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000286 | molecular_function | alanine dehydrogenase activity |
A | 0001666 | biological_process | response to hypoxia |
A | 0005576 | cellular_component | extracellular region |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006524 | biological_process | alanine catabolic process |
A | 0009274 | cellular_component | peptidoglycan-based cell wall |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0042853 | biological_process | L-alanine catabolic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0000286 | molecular_function | alanine dehydrogenase activity |
B | 0001666 | biological_process | response to hypoxia |
B | 0005576 | cellular_component | extracellular region |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0006524 | biological_process | alanine catabolic process |
B | 0009274 | cellular_component | peptidoglycan-based cell wall |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0042853 | biological_process | L-alanine catabolic process |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00836 |
Number of Residues | 27 |
Details | ALADH_PNT_1 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 1. GIPtEtknNEf..RVAiTPaGVaeLtRrG |
Chain | Residue | Details |
A | GLY4-GLY30 |
site_id | PS00837 |
Number of Residues | 26 |
Details | ALADH_PNT_2 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 2. VIGAGtAGynAariAnGMGAtVtvlD |
Chain | Residue | Details |
A | VAL173-ASP198 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:18304579 |
Chain | Residue | Details |
A | HIS96 | |
A | ASP270 | |
B | HIS96 | |
B | ASP270 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18304579 |
Chain | Residue | Details |
A | ARG15 | |
A | LYS75 | |
B | ARG15 | |
B | LYS75 |
site_id | SWS_FT_FI3 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18304579, ECO:0000269|PubMed:18491387 |
Chain | Residue | Details |
A | SER134 | |
B | SER134 | |
B | THR178 | |
B | ASP198 | |
B | LYS203 | |
B | SER220 | |
B | VAL239 | |
B | ILE267 | |
B | ARG279 | |
B | VAL298 | |
A | THR178 | |
A | ASP198 | |
A | LYS203 | |
A | SER220 | |
A | VAL239 | |
A | ILE267 | |
A | ARG279 | |
A | VAL298 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18304579, ECO:0007744|PDB:2VHX |
Chain | Residue | Details |
A | GLU323 | |
A | HIS327 | |
B | GLU323 | |
B | HIS327 |