3NJ4
Fluoro-neplanocin A in Human S-Adenosylhomocysteine Hydrolase
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 |
| C | 0004013 | molecular_function | adenosylhomocysteinase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0005829 | cellular_component | cytosol |
| C | 0006730 | biological_process | one-carbon metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0033353 | biological_process | S-adenosylmethionine cycle |
| C | 0042470 | cellular_component | melanosome |
| C | 0070062 | cellular_component | extracellular exosome |
| D | 0004013 | molecular_function | adenosylhomocysteinase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0005829 | cellular_component | cytosol |
| D | 0006730 | biological_process | one-carbon metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0033353 | biological_process | S-adenosylmethionine cycle |
| D | 0042470 | cellular_component | melanosome |
| D | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD A 501 |
| Chain | Residue |
| A | THR157 |
| A | THR242 |
| A | GLU243 |
| A | ILE244 |
| A | ASP245 |
| A | ASN248 |
| A | THR275 |
| A | THR276 |
| A | CYS278 |
| A | ILE281 |
| A | ILE299 |
| A | THR158 |
| A | GLY300 |
| A | HIS301 |
| A | LEU344 |
| A | ASN346 |
| A | HIS353 |
| A | HOH451 |
| A | HOH478 |
| A | HOH486 |
| A | AFX601 |
| B | LEU409 |
| A | THR159 |
| B | GLN413 |
| B | LYS426 |
| B | TYR430 |
| B | HOH457 |
| A | ASP190 |
| A | ASN191 |
| A | GLY220 |
| A | GLY222 |
| A | ASP223 |
| A | VAL224 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE AFX A 601 |
| Chain | Residue |
| A | HIS55 |
| A | THR57 |
| A | GLU59 |
| A | THR60 |
| A | ASP131 |
| A | GLU156 |
| A | THR157 |
| A | LYS186 |
| A | ASP190 |
| A | HIS301 |
| A | LEU344 |
| A | LEU347 |
| A | MET351 |
| A | GLY352 |
| A | HIS353 |
| A | MET358 |
| A | NAD501 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD B 502 |
| Chain | Residue |
| A | GLN413 |
| A | LYS426 |
| A | TYR430 |
| B | THR157 |
| B | THR158 |
| B | THR159 |
| B | ASP190 |
| B | ASN191 |
| B | GLY220 |
| B | GLY222 |
| B | ASP223 |
| B | VAL224 |
| B | THR242 |
| B | GLU243 |
| B | ILE244 |
| B | ASP245 |
| B | ASN248 |
| B | THR275 |
| B | THR276 |
| B | ILE281 |
| B | ILE299 |
| B | GLY300 |
| B | HIS301 |
| B | LEU344 |
| B | ASN346 |
| B | HIS353 |
| B | HOH512 |
| B | AFX602 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE AFX B 602 |
| Chain | Residue |
| B | LEU54 |
| B | HIS55 |
| B | THR57 |
| B | GLU59 |
| B | THR60 |
| B | ASP131 |
| B | GLU156 |
| B | THR157 |
| B | LYS186 |
| B | ASP190 |
| B | HIS301 |
| B | LEU347 |
| B | MET351 |
| B | GLY352 |
| B | HIS353 |
| B | MET358 |
| B | NAD502 |
| site_id | AC5 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD C 503 |
| Chain | Residue |
| C | ASN191 |
| C | GLY220 |
| C | GLY222 |
| C | ASP223 |
| C | VAL224 |
| C | THR242 |
| C | GLU243 |
| C | ILE244 |
| C | ASP245 |
| C | ASN248 |
| C | THR275 |
| C | THR276 |
| C | ILE281 |
| C | ILE299 |
| C | GLY300 |
| C | HIS301 |
| C | LEU344 |
| C | ASN346 |
| C | HIS353 |
| C | AFX603 |
| D | LEU409 |
| D | LYS426 |
| D | TYR430 |
| C | THR157 |
| C | THR158 |
| C | THR159 |
| C | ASP190 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AFX C 603 |
| Chain | Residue |
| C | HIS55 |
| C | THR57 |
| C | GLU59 |
| C | ASP131 |
| C | GLU156 |
| C | THR157 |
| C | LYS186 |
| C | ASP190 |
| C | HIS301 |
| C | LEU347 |
| C | MET351 |
| C | GLY352 |
| C | HIS353 |
| C | MET358 |
| C | NAD503 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD D 504 |
| Chain | Residue |
| C | GLN413 |
| C | LYS426 |
| C | TYR430 |
| D | THR157 |
| D | THR158 |
| D | THR159 |
| D | ASP190 |
| D | ASN191 |
| D | GLY220 |
| D | GLY222 |
| D | ASP223 |
| D | VAL224 |
| D | THR242 |
| D | GLU243 |
| D | ILE244 |
| D | ASP245 |
| D | ASN248 |
| D | THR275 |
| D | THR276 |
| D | ILE281 |
| D | ILE299 |
| D | HIS301 |
| D | LEU344 |
| D | ASN346 |
| D | HIS353 |
| D | HOH442 |
| D | HOH454 |
| D | AFX604 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE AFX D 604 |
| Chain | Residue |
| D | HIS55 |
| D | THR57 |
| D | GLU59 |
| D | THR60 |
| D | ASP131 |
| D | GLU156 |
| D | THR157 |
| D | LYS186 |
| D | ASP190 |
| D | HIS301 |
| D | LEU347 |
| D | MET351 |
| D | GLY352 |
| D | HIS353 |
| D | MET358 |
| D | NAD504 |
Functional Information from PROSITE/UniProt
| site_id | PS00738 |
| Number of Residues | 15 |
| Details | ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiFSTQDhAAAAI |
| 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 | 20 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P10760","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 52 |
| 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 | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| 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 | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P50247","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
