6QUE
Structure of ovine transhydrogenase in the presence of NADP+ in a "single face-down" conformation
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue NAP A 1101 |
| Chain | Residue |
| A | ALA786 |
| A | GLY964 |
| A | ASN966 |
| A | ASP967 |
| A | THR968 |
| A | LYS999 |
| A | ARG1000 |
| A | SER1001 |
| A | ASP1025 |
| A | ALA1026 |
| A | ASP787 |
| A | PRO789 |
| A | MET833 |
| A | MET837 |
| A | ALA895 |
| A | VAL922 |
| A | GLY924 |
| A | ARG925 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue NAD A 1102 |
| Chain | Residue |
| A | ARG139 |
| A | GLY192 |
| A | GLY193 |
| A | VAL194 |
| A | ASP214 |
| A | THR215 |
| A | ARG216 |
| A | GLY244 |
| A | TYR245 |
| A | ALA246 |
| A | GLU257 |
| A | ALA275 |
| A | LEU276 |
| A | ILE277 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue NAD B 1101 |
| Chain | Residue |
| B | ARG139 |
| B | VAL140 |
| B | GLY191 |
| B | GLY192 |
| B | GLY193 |
| B | VAL194 |
| B | ASP214 |
| B | THR215 |
| B | ARG216 |
| B | GLY244 |
| B | TYR245 |
| B | ALA246 |
| B | GLU257 |
| B | THR274 |
| B | ALA275 |
| B | LEU276 |
| B | ILE277 |
Functional Information from PROSITE/UniProt
| site_id | PS00836 |
| Number of Residues | 27 |
| Details | ALADH_PNT_1 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 1. GVPkEifqNEk..RVAlSPaGVqaLvKqG |
| Chain | Residue | Details |
| A | GLY17-GLY43 |
| site_id | PS00837 |
| Number of Residues | 26 |
| Details | ALADH_PNT_2 Alanine dehydrogenase & pyridine nucleotide transhydrogenase signature 2. IVGGGvAGlaSagaAkSMGAiVrgfD |
| Chain | Residue | Details |
| A | ILE189-ASP214 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 550 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"UniProtKB","id":"P11024","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 32 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"UniProtKB","id":"P11024","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31462775","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6QTI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6QUE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31462775","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6QUE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P07001","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q13423","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q13423","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 9 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q61941","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
