1XLT
Crystal structure of Transhydrogenase [(domain I)2:domain III] heterotrimer complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003957 | molecular_function | NAD(P)+ transhydrogenase (Si-specific) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006740 | biological_process | NADPH regeneration |
| A | 0008750 | molecular_function | proton-translocating NAD(P)+ transhydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046983 | molecular_function | protein dimerization activity |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070403 | molecular_function | NAD+ binding |
| A | 0070404 | molecular_function | NADH binding |
| A | 1902600 | biological_process | proton transmembrane transport |
| B | 0003957 | molecular_function | NAD(P)+ transhydrogenase (Si-specific) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006740 | biological_process | NADPH regeneration |
| B | 0008750 | molecular_function | proton-translocating NAD(P)+ transhydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046983 | molecular_function | protein dimerization activity |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
| B | 0070403 | molecular_function | NAD+ binding |
| B | 0070404 | molecular_function | NADH binding |
| B | 1902600 | biological_process | proton transmembrane transport |
| D | 0003957 | molecular_function | NAD(P)+ transhydrogenase (Si-specific) activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006740 | biological_process | NADPH regeneration |
| D | 0008750 | molecular_function | proton-translocating NAD(P)+ transhydrogenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046983 | molecular_function | protein dimerization activity |
| D | 0050661 | molecular_function | NADP binding |
| D | 0051287 | molecular_function | NAD binding |
| D | 0070403 | molecular_function | NAD+ binding |
| D | 0070404 | molecular_function | NADH binding |
| D | 1902600 | biological_process | proton transmembrane transport |
| E | 0003957 | molecular_function | NAD(P)+ transhydrogenase (Si-specific) activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0006740 | biological_process | NADPH regeneration |
| E | 0008750 | molecular_function | proton-translocating NAD(P)+ transhydrogenase activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0046983 | molecular_function | protein dimerization activity |
| E | 0050661 | molecular_function | NADP binding |
| E | 0051287 | molecular_function | NAD binding |
| E | 0070403 | molecular_function | NAD+ binding |
| E | 0070404 | molecular_function | NADH binding |
| E | 1902600 | biological_process | proton transmembrane transport |
| G | 0003957 | molecular_function | NAD(P)+ transhydrogenase (Si-specific) activity |
| G | 0005515 | molecular_function | protein binding |
| G | 0005886 | cellular_component | plasma membrane |
| G | 0006740 | biological_process | NADPH regeneration |
| G | 0008750 | molecular_function | proton-translocating NAD(P)+ transhydrogenase activity |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0046983 | molecular_function | protein dimerization activity |
| G | 0050661 | molecular_function | NADP binding |
| G | 0051287 | molecular_function | NAD binding |
| G | 0070403 | molecular_function | NAD+ binding |
| G | 0070404 | molecular_function | NADH binding |
| G | 1902600 | biological_process | proton transmembrane transport |
| H | 0003957 | molecular_function | NAD(P)+ transhydrogenase (Si-specific) activity |
| H | 0005515 | molecular_function | protein binding |
| H | 0005886 | cellular_component | plasma membrane |
| H | 0006740 | biological_process | NADPH regeneration |
| H | 0008750 | molecular_function | proton-translocating NAD(P)+ transhydrogenase activity |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0046983 | molecular_function | protein dimerization activity |
| H | 0050661 | molecular_function | NADP binding |
| H | 0051287 | molecular_function | NAD binding |
| H | 0070403 | molecular_function | NAD+ binding |
| H | 0070404 | molecular_function | NADH binding |
| H | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PROSITE/UniProt
| site_id | PS00836 |
| Number of Residues | 27 |
| Details | ALADH_PNT_1 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 1. AIPkErrpGEd..RVAiSPeVVkkLvGlG |
| Chain | Residue | Details |
| A | ALA4-GLY30 |
| site_id | PS00837 |
| Number of Residues | 26 |
| Details | ALADH_PNT_2 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 2. VFGVGvAGlqAiatAkRLGAvVmatD |
| Chain | Residue | Details |
| A | VAL177-ASP202 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 60 |
| Details | Region: {"description":"RQD loop; involved in interaction with PntB"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 67 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10997900","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11250201","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15670609","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 54 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12791694","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15323555","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PTJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U2G","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1djl |
| Chain | Residue | Details |
| C | TYR316 | |
| C | TYR432 | |
| C | ARG351 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1djl |
| Chain | Residue | Details |
| F | TYR316 | |
| F | TYR432 | |
| F | ARG351 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1djl |
| Chain | Residue | Details |
| I | TYR316 | |
| I | TYR432 | |
| I | ARG351 |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 116 |
| Chain | Residue | Details |
| C | ASP393 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLN132 | steric locator |
| A | ASP135 | hydrogen bond acceptor, steric role |
| A | SER138 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 116 |
| Chain | Residue | Details |
| F | ASP393 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLN132 | steric locator |
| B | ASP135 | hydrogen bond acceptor, steric role |
| B | SER138 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 1 |
| Details | M-CSA 116 |
| Chain | Residue | Details |
| I | ASP393 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | GLN132 | steric locator |
| D | ASP135 | hydrogen bond acceptor, steric role |
| D | SER138 | electrostatic stabiliser |
| D | TYR235 | polar/non-polar interaction, steric role |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 116 |
| Chain | Residue | Details |
| E | ARG127 | hydrogen bond donor, steric role |
| E | GLN132 | steric locator |
| E | ASP135 | hydrogen bond acceptor, steric role |
| E | SER138 | electrostatic stabiliser |
| site_id | MCSA5 |
| Number of Residues | 4 |
| Details | M-CSA 116 |
| Chain | Residue | Details |
| G | ARG127 | hydrogen bond donor, steric role |
| G | GLN132 | steric locator |
| G | ASP135 | hydrogen bond acceptor, steric role |
| G | SER138 | electrostatic stabiliser |
| site_id | MCSA6 |
| Number of Residues | 4 |
| Details | M-CSA 116 |
| Chain | Residue | Details |
| H | ARG127 | hydrogen bond donor, steric role |
| H | GLN132 | steric locator |
| H | ASP135 | hydrogen bond acceptor, steric role |
| H | SER138 | electrostatic stabiliser |






