1SO8
Abeta-bound human ABAD structure [also known as 3-hydroxyacyl-CoA dehydrogenase type II (Type II HADH), Endoplasmic reticulum-associated amyloid beta-peptide binding protein (ERAB)]
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000049 | molecular_function | tRNA binding |
A | 0003723 | molecular_function | RNA binding |
A | 0003857 | molecular_function | 3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
A | 0004303 | molecular_function | estradiol 17-beta-dehydrogenase [NAD(P)+] activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0005886 | cellular_component | plasma membrane |
A | 0006550 | biological_process | L-isoleucine catabolic process |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006635 | biological_process | fatty acid beta-oxidation |
A | 0006699 | biological_process | bile acid biosynthetic process |
A | 0007005 | biological_process | mitochondrion organization |
A | 0008033 | biological_process | tRNA processing |
A | 0008202 | biological_process | steroid metabolic process |
A | 0008207 | biological_process | C21-steroid hormone metabolic process |
A | 0008209 | biological_process | androgen metabolic process |
A | 0008210 | biological_process | estrogen metabolic process |
A | 0008709 | molecular_function | cholate 7-alpha-dehydrogenase (NAD+) activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0030283 | molecular_function | testosterone dehydrogenase [NAD(P)+] activity |
A | 0030678 | cellular_component | mitochondrial ribonuclease P complex |
A | 0042645 | cellular_component | mitochondrial nucleoid |
A | 0043527 | cellular_component | tRNA methyltransferase complex |
A | 0044594 | molecular_function | 17-beta-hydroxysteroid dehydrogenase (NAD+) activity |
A | 0047015 | molecular_function | 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity |
A | 0047035 | molecular_function | testosterone dehydrogenase (NAD+) activity |
A | 0047044 | molecular_function | androstan-3-alpha,17-beta-diol dehydrogenase (NAD+) activity |
A | 0051289 | biological_process | protein homotetramerization |
A | 0062173 | biological_process | brexanolone metabolic process |
A | 0070901 | biological_process | mitochondrial tRNA methylation |
A | 0097745 | biological_process | mitochondrial tRNA 5'-end processing |
A | 0106281 | molecular_function | chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity |
A | 0106282 | molecular_function | isoursodeoxycholate 7-beta-dehydrogenase (NAD+) activity |
A | 0106283 | molecular_function | ursodeoxycholate 7-beta-dehydrogenase (NAD+) activity |
A | 1990180 | biological_process | mitochondrial tRNA 3'-end processing |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 301 |
Chain | Residue |
A | SER67 |
A | SER67 |
A | GLU68 |
A | GLU68 |
A | LYS69 |
A | LYS69 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 302 |
Chain | Residue |
A | HOH545 |
A | HOH560 |
A | HOH602 |
A | GLY17 |
A | SER20 |
A | HOH522 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL A 303 |
Chain | Residue |
A | ALA154 |
A | SER155 |
A | GLY173 |
A | ILE175 |
A | VAL176 |
A | HOH570 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvaafegqvgQaaYSASKGGIvGMTlPIA |
Chain | Residue | Details |
A | SER155-ALA183 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15087549","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"15342248","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1U7T","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"15087549","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"O08756","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O08756","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
A | LYS172 | |
A | SER155 | |
A | ASN121 | |
A | TYR168 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
A | LYS172 | |
A | GLN165 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
A | LYS172 | |
A | TYR168 |