5W4B
The crystal structure of human S-adenosylhomocysteine hydrolase (AHCY) bound to benzothiazole inhibitor
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 |
E | 0004013 | molecular_function | adenosylhomocysteinase activity |
E | 0005515 | molecular_function | protein binding |
E | 0005634 | cellular_component | nucleus |
E | 0005737 | cellular_component | cytoplasm |
E | 0005783 | cellular_component | endoplasmic reticulum |
E | 0005829 | cellular_component | cytosol |
E | 0006730 | biological_process | one-carbon metabolic process |
E | 0016787 | molecular_function | hydrolase activity |
E | 0033353 | biological_process | S-adenosylmethionine cycle |
E | 0042470 | cellular_component | melanosome |
E | 0070062 | cellular_component | extracellular exosome |
F | 0004013 | molecular_function | adenosylhomocysteinase activity |
F | 0005515 | molecular_function | protein binding |
F | 0005634 | cellular_component | nucleus |
F | 0005737 | cellular_component | cytoplasm |
F | 0005783 | cellular_component | endoplasmic reticulum |
F | 0005829 | cellular_component | cytosol |
F | 0006730 | biological_process | one-carbon metabolic process |
F | 0016787 | molecular_function | hydrolase activity |
F | 0033353 | biological_process | S-adenosylmethionine cycle |
F | 0042470 | cellular_component | melanosome |
F | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 27 |
Details | binding site for residue NAD A 501 |
Chain | Residue |
A | ASP190 |
A | ASN248 |
A | THR275 |
A | THR276 |
A | GLY277 |
A | CYS278 |
A | ILE281 |
A | ILE299 |
A | GLY300 |
A | HIS301 |
A | LEU344 |
A | ASN191 |
A | ASN346 |
A | HOH611 |
A | HOH634 |
A | HOH649 |
A | HOH682 |
B | GLN413 |
B | LYS426 |
B | TYR430 |
A | GLY222 |
A | ASP223 |
A | VAL224 |
A | THR242 |
A | GLU243 |
A | ILE244 |
A | ASP245 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue 9W4 A 502 |
Chain | Residue |
A | HIS55 |
A | THR57 |
A | GLU59 |
A | ASN80 |
A | GLN324 |
A | ARG343 |
A | LEU347 |
A | HIS353 |
A | MET358 |
A | HOH645 |
site_id | AC3 |
Number of Residues | 30 |
Details | binding site for residue NAD B 501 |
Chain | Residue |
A | GLN413 |
A | LYS426 |
A | TYR430 |
B | ASP190 |
B | ASN191 |
B | GLY222 |
B | ASP223 |
B | VAL224 |
B | THR242 |
B | GLU243 |
B | ILE244 |
B | ASP245 |
B | ASN248 |
B | THR275 |
B | THR276 |
B | GLY277 |
B | CYS278 |
B | ILE281 |
B | ILE299 |
B | GLY300 |
B | HIS301 |
B | LEU344 |
B | ASN346 |
B | HOH616 |
B | HOH631 |
B | HOH652 |
B | HOH664 |
B | HOH684 |
B | HOH695 |
B | HOH706 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for residue 9W4 B 502 |
Chain | Residue |
B | HIS55 |
B | THR57 |
B | GLU59 |
B | ASN80 |
B | PHE82 |
B | SER83 |
B | GLN324 |
B | ARG343 |
B | LEU347 |
B | HIS353 |
B | MET358 |
B | HOH611 |
site_id | AC5 |
Number of Residues | 29 |
Details | binding site for residue NAD C 501 |
Chain | Residue |
C | HOH644 |
C | HOH651 |
C | HOH656 |
C | HOH673 |
C | HOH681 |
C | HOH685 |
D | GLN413 |
D | LYS426 |
D | TYR430 |
C | ASP190 |
C | ASN191 |
C | GLY222 |
C | ASP223 |
C | VAL224 |
C | THR242 |
C | GLU243 |
C | ILE244 |
C | ASP245 |
C | ASN248 |
C | THR275 |
C | THR276 |
C | GLY277 |
C | CYS278 |
C | ILE281 |
C | ILE299 |
C | GLY300 |
C | HIS301 |
C | ASN346 |
C | HOH601 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue 9W4 C 502 |
Chain | Residue |
C | HIS55 |
C | THR57 |
C | GLU59 |
C | ASN80 |
C | ARG343 |
C | LEU347 |
C | HIS353 |
C | MET358 |
site_id | AC7 |
Number of Residues | 29 |
Details | binding site for residue NAD D 501 |
Chain | Residue |
C | GLN413 |
C | LYS426 |
C | TYR430 |
D | ASP190 |
D | ASN191 |
D | GLY222 |
D | ASP223 |
D | VAL224 |
D | THR242 |
D | GLU243 |
D | ILE244 |
D | ASP245 |
D | ASN248 |
D | THR275 |
D | THR276 |
D | GLY277 |
D | CYS278 |
D | ILE281 |
D | ILE299 |
D | GLY300 |
D | HIS301 |
D | ASN346 |
D | HOH608 |
D | HOH644 |
D | HOH658 |
D | HOH682 |
D | HOH691 |
D | HOH718 |
D | HOH734 |
site_id | AC8 |
Number of Residues | 10 |
Details | binding site for residue 9W4 D 502 |
Chain | Residue |
D | HIS55 |
D | THR57 |
D | GLU59 |
D | ASN80 |
D | PHE82 |
D | GLN324 |
D | ARG343 |
D | LEU347 |
D | HIS353 |
D | MET358 |
site_id | AC9 |
Number of Residues | 29 |
Details | binding site for residue NAD E 501 |
Chain | Residue |
E | ASP190 |
E | ASN191 |
E | GLY222 |
E | ASP223 |
E | VAL224 |
E | THR242 |
E | GLU243 |
E | ILE244 |
E | ASP245 |
E | ASN248 |
E | THR275 |
E | THR276 |
E | GLY277 |
E | CYS278 |
E | ILE281 |
E | ILE299 |
E | GLY300 |
E | HIS301 |
E | LEU344 |
E | ASN346 |
E | HOH619 |
E | HOH623 |
E | HOH651 |
E | HOH673 |
E | HOH684 |
E | HOH685 |
F | GLN413 |
F | LYS426 |
F | TYR430 |
site_id | AD1 |
Number of Residues | 13 |
Details | binding site for residue 9W4 E 502 |
Chain | Residue |
E | HIS55 |
E | THR57 |
E | GLU59 |
E | ASN80 |
E | SER83 |
E | GLN324 |
E | ARG343 |
E | LEU347 |
E | HIS353 |
E | MET358 |
E | EDO503 |
E | HOH696 |
E | HOH732 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue EDO E 503 |
Chain | Residue |
E | ARG343 |
E | LEU344 |
E | 9W4502 |
E | HOH620 |
site_id | AD3 |
Number of Residues | 29 |
Details | binding site for residue NAD F 501 |
Chain | Residue |
E | GLN413 |
E | LYS426 |
E | TYR430 |
F | ASP190 |
F | ASN191 |
F | GLY222 |
F | ASP223 |
F | VAL224 |
F | GLU243 |
F | ILE244 |
F | ASP245 |
F | ASN248 |
F | THR275 |
F | THR276 |
F | GLY277 |
F | CYS278 |
F | ILE281 |
F | ILE299 |
F | GLY300 |
F | HIS301 |
F | ASN346 |
F | HIS353 |
F | HOH656 |
F | HOH675 |
F | HOH677 |
F | HOH696 |
F | HOH703 |
F | HOH714 |
F | HOH724 |
site_id | AD4 |
Number of Residues | 14 |
Details | binding site for residue 9W4 F 502 |
Chain | Residue |
F | HIS55 |
F | THR57 |
F | GLU59 |
F | ASN80 |
F | PHE82 |
F | SER83 |
F | GLN324 |
F | ARG343 |
F | LEU347 |
F | MET351 |
F | HIS353 |
F | MET358 |
F | HOH640 |
F | HOH644 |
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 | 30 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P10760 |
Chain | Residue | Details |
A | THR57 | |
B | ASP190 | |
C | THR57 | |
C | ASP131 | |
C | GLU156 | |
C | LYS186 | |
C | ASP190 | |
D | THR57 | |
D | ASP131 | |
D | GLU156 | |
D | LYS186 | |
A | ASP131 | |
D | ASP190 | |
E | THR57 | |
E | ASP131 | |
E | GLU156 | |
E | LYS186 | |
E | ASP190 | |
F | THR57 | |
F | ASP131 | |
F | GLU156 | |
F | LYS186 | |
A | GLU156 | |
F | ASP190 | |
A | LYS186 | |
A | ASP190 | |
B | THR57 | |
B | ASP131 | |
B | GLU156 | |
B | LYS186 |
site_id | SWS_FT_FI2 |
Number of Residues | 42 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12590576, ECO:0000269|PubMed:9586999 |
Chain | Residue | Details |
A | THR157 | |
B | GLU243 | |
B | ASN248 | |
B | ILE299 | |
B | ASN346 | |
B | HIS353 | |
C | THR157 | |
C | GLY222 | |
C | GLU243 | |
C | ASN248 | |
C | ILE299 | |
A | GLY222 | |
C | ASN346 | |
C | HIS353 | |
D | THR157 | |
D | GLY222 | |
D | GLU243 | |
D | ASN248 | |
D | ILE299 | |
D | ASN346 | |
D | HIS353 | |
E | THR157 | |
A | GLU243 | |
E | GLY222 | |
E | GLU243 | |
E | ASN248 | |
E | ILE299 | |
E | ASN346 | |
E | HIS353 | |
F | THR157 | |
F | GLY222 | |
F | GLU243 | |
F | ASN248 | |
A | ASN248 | |
F | ILE299 | |
F | ASN346 | |
F | HIS353 | |
A | ILE299 | |
A | ASN346 | |
A | HIS353 | |
B | THR157 | |
B | GLY222 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER183 | |
B | SER183 | |
C | SER183 | |
D | SER183 | |
E | SER183 | |
F | SER183 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 |
Chain | Residue | Details |
A | LYS186 | |
B | LYS186 | |
C | LYS186 | |
D | LYS186 | |
E | LYS186 | |
F | LYS186 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P50247 |
Chain | Residue | Details |
A | TYR193 | |
B | TYR193 | |
C | TYR193 | |
D | TYR193 | |
E | TYR193 | |
F | TYR193 |