2VHX
Crystal structure of the ternary complex of L-alanine dehydrogenase from Mycobacterium tuberculosis with NAD+ and pyruvate
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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000286 | molecular_function | alanine dehydrogenase activity |
| C | 0001666 | biological_process | response to hypoxia |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005829 | cellular_component | cytosol |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006524 | biological_process | alanine catabolic process |
| C | 0009274 | cellular_component | peptidoglycan-based cell wall |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0042853 | biological_process | L-alanine catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000286 | molecular_function | alanine dehydrogenase activity |
| D | 0001666 | biological_process | response to hypoxia |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005829 | cellular_component | cytosol |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006524 | biological_process | alanine catabolic process |
| D | 0009274 | cellular_component | peptidoglycan-based cell wall |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0042853 | biological_process | L-alanine catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0000286 | molecular_function | alanine dehydrogenase activity |
| E | 0001666 | biological_process | response to hypoxia |
| E | 0005576 | cellular_component | extracellular region |
| E | 0005829 | cellular_component | cytosol |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0006524 | biological_process | alanine catabolic process |
| E | 0009274 | cellular_component | peptidoglycan-based cell wall |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0042853 | biological_process | L-alanine catabolic process |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0000286 | molecular_function | alanine dehydrogenase activity |
| F | 0001666 | biological_process | response to hypoxia |
| F | 0005576 | cellular_component | extracellular region |
| F | 0005829 | cellular_component | cytosol |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0006524 | biological_process | alanine catabolic process |
| F | 0009274 | cellular_component | peptidoglycan-based cell wall |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0042853 | biological_process | L-alanine catabolic process |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A1372 |
| Chain | Residue |
| A | GLU323 |
| A | HIS327 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG B1372 |
| Chain | Residue |
| B | HIS327 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG F1374 |
| Chain | Residue |
| F | GLU323 |
| F | HIS327 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PYR F1375 |
| Chain | Residue |
| F | MET133 |
| F | ASP270 |
| F | ALA299 |
| F | ASN300 |
| F | PRO302 |
| F | NAD1376 |
| F | ARG15 |
| F | LYS75 |
| F | HIS96 |
| F | LEU130 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PYR E1374 |
| Chain | Residue |
| E | ARG15 |
| E | LYS75 |
| E | HIS96 |
| E | MET133 |
| E | ASP270 |
| E | ALA299 |
| E | ASN300 |
| E | PRO302 |
| E | NAD1375 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PYR B1373 |
| Chain | Residue |
| B | ARG15 |
| B | LYS75 |
| B | PHE94 |
| B | HIS96 |
| B | LEU130 |
| B | MET133 |
| B | ASN300 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PYR D1371 |
| Chain | Residue |
| D | ARG15 |
| D | LYS75 |
| D | HIS96 |
| D | LEU130 |
| D | MET133 |
| D | ASN300 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PYR A1373 |
| Chain | Residue |
| A | ARG15 |
| A | LYS75 |
| A | PHE94 |
| A | HIS96 |
| A | MET133 |
| A | ASP270 |
| A | ASN300 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PYR C1371 |
| Chain | Residue |
| C | ARG15 |
| C | LYS75 |
| C | HIS96 |
| C | LEU130 |
| C | MET133 |
| C | ASN300 |
| site_id | BC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD E1375 |
| Chain | Residue |
| E | LEU130 |
| E | MET133 |
| E | SER134 |
| E | ALA137 |
| E | GLY177 |
| E | THR178 |
| E | ALA179 |
| E | ASP198 |
| E | LYS203 |
| E | SER220 |
| E | ALA238 |
| E | VAL239 |
| E | LEU240 |
| E | LEU249 |
| E | ILE267 |
| E | ASP270 |
| E | GLN271 |
| E | VAL298 |
| E | ALA299 |
| E | ASN300 |
| E | MET301 |
| E | PRO302 |
| E | PYR1374 |
| E | HOH2098 |
| E | HOH2116 |
| E | HOH2125 |
| E | HOH2190 |
| E | HOH2191 |
| E | HOH2192 |
| E | HOH2193 |
| E | HOH2194 |
| E | HOH2195 |
| site_id | BC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD F1376 |
| Chain | Residue |
| F | ASN300 |
| F | MET301 |
| F | PRO302 |
| F | PYR1375 |
| F | HOH2131 |
| F | HOH2145 |
| F | HOH2158 |
| F | HOH2246 |
| F | HOH2247 |
| F | HOH2248 |
| F | HOH2250 |
| F | HOH2251 |
| F | HOH2252 |
| F | MET133 |
| F | SER134 |
| F | ALA137 |
| F | GLY177 |
| F | THR178 |
| F | ALA179 |
| F | ASP198 |
| F | LYS203 |
| F | SER220 |
| F | ALA238 |
| F | VAL239 |
| F | LEU240 |
| F | ILE267 |
| F | ASP270 |
| F | GLN271 |
| F | VAL298 |
| F | ALA299 |
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 | 12 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:18304579 |
| Chain | Residue | Details |
| A | HIS96 | |
| A | ASP270 | |
| B | HIS96 | |
| B | ASP270 | |
| C | HIS96 | |
| C | ASP270 | |
| D | HIS96 | |
| D | ASP270 | |
| E | HIS96 | |
| E | ASP270 | |
| F | HIS96 | |
| F | ASP270 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18304579 |
| Chain | Residue | Details |
| A | ARG15 | |
| A | LYS75 | |
| B | ARG15 | |
| B | LYS75 | |
| C | ARG15 | |
| C | LYS75 | |
| D | ARG15 | |
| D | LYS75 | |
| E | ARG15 | |
| E | LYS75 | |
| F | ARG15 | |
| F | LYS75 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 54 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18304579, ECO:0000269|PubMed:18491387 |
| Chain | Residue | Details |
| A | ILE267 | |
| A | ARG279 | |
| A | VAL298 | |
| B | SER134 | |
| B | THR178 | |
| B | ASP198 | |
| B | LYS203 | |
| B | SER220 | |
| B | VAL239 | |
| B | ILE267 | |
| B | ARG279 | |
| B | VAL298 | |
| C | SER134 | |
| C | THR178 | |
| C | ASP198 | |
| C | LYS203 | |
| C | SER220 | |
| C | VAL239 | |
| C | ILE267 | |
| C | ARG279 | |
| C | VAL298 | |
| D | SER134 | |
| D | THR178 | |
| D | ASP198 | |
| D | LYS203 | |
| D | SER220 | |
| D | VAL239 | |
| D | ILE267 | |
| D | ARG279 | |
| D | VAL298 | |
| E | SER134 | |
| E | THR178 | |
| E | ASP198 | |
| E | LYS203 | |
| E | SER220 | |
| E | VAL239 | |
| E | ILE267 | |
| E | ARG279 | |
| E | VAL298 | |
| F | SER134 | |
| F | THR178 | |
| F | ASP198 | |
| F | LYS203 | |
| F | SER220 | |
| F | VAL239 | |
| F | ILE267 | |
| F | ARG279 | |
| F | VAL298 | |
| A | SER134 | |
| A | THR178 | |
| A | ASP198 | |
| A | LYS203 | |
| A | SER220 | |
| A | VAL239 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18304579, ECO:0007744|PDB:2VHX |
| Chain | Residue | Details |
| D | GLU323 | |
| D | HIS327 | |
| E | GLU323 | |
| E | HIS327 | |
| F | GLU323 | |
| F | HIS327 | |
| A | GLU323 | |
| A | HIS327 | |
| B | GLU323 | |
| B | HIS327 | |
| C | GLU323 | |
| C | HIS327 |
