1A7A
STRUCTURE OF HUMAN PLACENTAL S-ADENOSYLHOMOCYSTEINE HYDROLASE: DETERMINATION OF A 30 SELENIUM ATOM SUBSTRUCTURE FROM DATA AT A SINGLE WAVELENGTH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004013 | molecular_function | adenosylhomocysteinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005829 | cellular_component | cytosol |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0033353 | biological_process | S-adenosylmethionine cycle |
| A | 0042470 | cellular_component | melanosome |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0004013 | molecular_function | adenosylhomocysteinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005829 | cellular_component | cytosol |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0033353 | biological_process | S-adenosylmethionine cycle |
| B | 0042470 | cellular_component | melanosome |
| B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD A 433 |
| Chain | Residue |
| A | THR157 |
| A | GLU243 |
| A | ILE244 |
| A | ASP245 |
| A | ASN248 |
| A | THR275 |
| A | THR276 |
| A | CYS278 |
| A | ILE281 |
| A | ILE299 |
| A | GLY300 |
| A | THR158 |
| A | HIS301 |
| A | ASN346 |
| A | HIS353 |
| A | ADC435 |
| A | HOH459 |
| B | GLN413 |
| B | LYS426 |
| B | TYR430 |
| A | THR159 |
| A | ASP190 |
| A | ASN191 |
| A | GLY220 |
| A | GLY222 |
| A | ASP223 |
| A | VAL224 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD B 434 |
| Chain | Residue |
| A | GLN413 |
| A | LYS426 |
| A | TYR430 |
| B | THR157 |
| B | THR158 |
| B | THR159 |
| B | ASN191 |
| B | GLY220 |
| B | GLY222 |
| B | ASP223 |
| B | VAL224 |
| B | GLU243 |
| B | ILE244 |
| B | ASP245 |
| B | ASN248 |
| B | THR275 |
| B | THR276 |
| B | CYS278 |
| B | ILE281 |
| B | ILE299 |
| B | GLY300 |
| B | HIS301 |
| B | ASN346 |
| B | HIS353 |
| B | ADC436 |
| B | HOH440 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADC A 435 |
| Chain | Residue |
| A | LEU54 |
| A | HIS55 |
| A | THR57 |
| A | GLU59 |
| A | THR60 |
| A | GLU156 |
| A | THR157 |
| A | LYS186 |
| A | ASP190 |
| A | LEU347 |
| A | MSE351 |
| A | HIS353 |
| A | MSE358 |
| A | NAD433 |
| A | HOH436 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADC B 436 |
| Chain | Residue |
| B | HIS55 |
| B | THR57 |
| B | GLU59 |
| B | THR60 |
| B | GLU156 |
| B | THR157 |
| B | LYS186 |
| B | ASP190 |
| B | MSE351 |
| B | HIS353 |
| B | MSE358 |
| B | NAD434 |
| B | HOH454 |
Functional Information from PROSITE/UniProt
| site_id | PS00738 |
| Number of Residues | 15 |
| Details | ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiFSTQNhAAAAI |
| Chain | Residue | Details |
| A | SER78-ILE92 |
| site_id | PS00739 |
| Number of Residues | 17 |
| Details | ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKvavVaGYGdVGKGc.A |
| Chain | Residue | Details |
| A | GLY213-ALA229 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P10760","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12590576","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9586999","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Heiserich L.","Gottlieb E."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29192674","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P50247","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| A | CYS195 | |
| A | LYS186 | |
| A | ASP131 | |
| A | ASN191 | |
| A | HIS55 | |
| A | ASP190 | |
| A | HIS301 |
| site_id | CSA2 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| B | CYS195 | |
| B | LYS186 | |
| B | ASP131 | |
| B | ASN191 | |
| B | HIS55 | |
| B | ASP190 | |
| B | HIS301 |
