1U28
R. rubrum transhydrogenase asymmetric complex (dI.NAD+)2(dIII.NADP+)1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD A 500 |
| Chain | Residue |
| A | PRO126 |
| A | VAL182 |
| A | ASP202 |
| A | VAL203 |
| A | ARG204 |
| A | GLY234 |
| A | ALA236 |
| A | GLN247 |
| A | THR264 |
| A | ALA265 |
| A | LEU266 |
| A | ARG127 |
| A | PRO273 |
| A | HOH508 |
| A | HOH520 |
| A | ILE128 |
| A | SER129 |
| A | ASP135 |
| A | LEU137 |
| A | SER138 |
| A | VAL180 |
| A | GLY181 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE NAD B 600 |
| Chain | Residue |
| B | GLY179 |
| B | VAL180 |
| B | GLY181 |
| B | VAL182 |
| B | ASP202 |
| B | VAL203 |
| B | ARG204 |
| B | THR264 |
| B | ALA265 |
| B | LEU266 |
| B | PRO273 |
| B | LEU275 |
| B | HOH819 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAP C 400 |
| Chain | Residue |
| B | GLN132 |
| C | GLY54 |
| C | TYR55 |
| C | GLY56 |
| C | ALA60 |
| C | VAL87 |
| C | ALA88 |
| C | GLY89 |
| C | ARG90 |
| C | MET91 |
| C | PRO92 |
| C | GLY129 |
| C | ALA130 |
| C | ASN131 |
| C | ASP132 |
| C | VAL133 |
| C | LYS164 |
| C | ARG165 |
| C | SER166 |
| C | ALA168 |
| C | SER169 |
| C | GLY170 |
| C | TYR171 |
| C | ASP190 |
| C | ALA191 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 700 |
| Chain | Residue |
| B | ARG15 |
| B | HIS99 |
| B | GLU296 |
| B | ASN322 |
| B | GOL800 |
| B | HOH825 |
| B | HOH846 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 800 |
| Chain | Residue |
| B | ARG10 |
| B | GLN75 |
| B | ARG76 |
| B | HIS99 |
| B | GLY101 |
| B | GOL700 |
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 | 20 |
| Details | Region: {"description":"RQD loop; involved in interaction with PntB"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 23 |
| 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 | 18 |
| 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 | ARG90 | |
| C | TYR171 | |
| C | TYR55 |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 116 |
| Chain | Residue | Details |
| C | ASP132 | 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 |
| A | TYR235 | polar/non-polar interaction, steric role |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 116 |
| Chain | Residue | Details |
| B | ARG127 | hydrogen bond donor, steric role |
| B | GLN132 | steric locator |
| B | ASP135 | hydrogen bond acceptor, steric role |
| B | SER138 | electrostatic stabiliser |
