1XWF
K185N mutated S-adenosylhomocysteine hydrolase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001666 | biological_process | response to hypoxia |
| A | 0002439 | biological_process | chronic inflammatory response to antigenic stimulus |
| A | 0004013 | molecular_function | adenosylhomocysteinase activity |
| A | 0005507 | molecular_function | copper ion 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 | 0007584 | biological_process | response to nutrient |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019510 | biological_process | S-adenosylhomocysteine catabolic process |
| A | 0030554 | molecular_function | adenyl nucleotide binding |
| A | 0033353 | biological_process | S-adenosylmethionine cycle |
| A | 0042470 | cellular_component | melanosome |
| A | 0042745 | biological_process | circadian sleep/wake cycle |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0051287 | molecular_function | NAD binding |
| A | 0098604 | molecular_function | adenosylselenohomocysteinase activity |
| B | 0001666 | biological_process | response to hypoxia |
| B | 0002439 | biological_process | chronic inflammatory response to antigenic stimulus |
| B | 0004013 | molecular_function | adenosylhomocysteinase activity |
| B | 0005507 | molecular_function | copper ion 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 | 0007584 | biological_process | response to nutrient |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019510 | biological_process | S-adenosylhomocysteine catabolic process |
| B | 0030554 | molecular_function | adenyl nucleotide binding |
| B | 0033353 | biological_process | S-adenosylmethionine cycle |
| B | 0042470 | cellular_component | melanosome |
| B | 0042745 | biological_process | circadian sleep/wake cycle |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0051287 | molecular_function | NAD binding |
| B | 0098604 | molecular_function | adenosylselenohomocysteinase activity |
| C | 0001666 | biological_process | response to hypoxia |
| C | 0002439 | biological_process | chronic inflammatory response to antigenic stimulus |
| C | 0004013 | molecular_function | adenosylhomocysteinase activity |
| C | 0005507 | molecular_function | copper ion 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 | 0007584 | biological_process | response to nutrient |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0019510 | biological_process | S-adenosylhomocysteine catabolic process |
| C | 0030554 | molecular_function | adenyl nucleotide binding |
| C | 0033353 | biological_process | S-adenosylmethionine cycle |
| C | 0042470 | cellular_component | melanosome |
| C | 0042745 | biological_process | circadian sleep/wake cycle |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0051287 | molecular_function | NAD binding |
| C | 0098604 | molecular_function | adenosylselenohomocysteinase activity |
| D | 0001666 | biological_process | response to hypoxia |
| D | 0002439 | biological_process | chronic inflammatory response to antigenic stimulus |
| D | 0004013 | molecular_function | adenosylhomocysteinase activity |
| D | 0005507 | molecular_function | copper ion 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 | 0007584 | biological_process | response to nutrient |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0019510 | biological_process | S-adenosylhomocysteine catabolic process |
| D | 0030554 | molecular_function | adenyl nucleotide binding |
| D | 0033353 | biological_process | S-adenosylmethionine cycle |
| D | 0042470 | cellular_component | melanosome |
| D | 0042745 | biological_process | circadian sleep/wake cycle |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0051287 | molecular_function | NAD binding |
| D | 0098604 | molecular_function | adenosylselenohomocysteinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD A 432 |
| Chain | Residue |
| A | THR157 |
| A | ILE243 |
| A | ASP244 |
| A | ASN247 |
| A | THR274 |
| A | THR275 |
| A | GLY276 |
| A | CYS277 |
| A | ILE280 |
| A | ILE298 |
| A | GLY299 |
| A | ASP189 |
| A | HIS300 |
| A | LEU343 |
| A | ASN345 |
| A | HIS352 |
| B | GLN412 |
| B | LYS425 |
| B | TYR429 |
| A | ASN190 |
| A | GLY219 |
| A | GLY221 |
| A | ASP222 |
| A | VAL223 |
| A | THR241 |
| A | GLU242 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADN A 433 |
| Chain | Residue |
| A | HIS54 |
| A | THR56 |
| A | GLU58 |
| A | ASP130 |
| A | GLU155 |
| A | ASP189 |
| A | HIS300 |
| A | LEU343 |
| A | LEU346 |
| A | HIS352 |
| A | MET357 |
| A | PHE361 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD B 432 |
| Chain | Residue |
| A | GLN412 |
| A | LYS425 |
| A | TYR429 |
| B | THR157 |
| B | ASP189 |
| B | ASN190 |
| B | GLY221 |
| B | ASP222 |
| B | VAL223 |
| B | THR241 |
| B | GLU242 |
| B | ILE243 |
| B | ASP244 |
| B | ASN247 |
| B | THR274 |
| B | THR275 |
| B | GLY276 |
| B | CYS277 |
| B | ILE280 |
| B | ILE298 |
| B | GLY299 |
| B | HIS300 |
| B | LEU343 |
| B | ASN345 |
| B | HIS352 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADN B 433 |
| Chain | Residue |
| B | LEU53 |
| B | HIS54 |
| B | THR56 |
| B | GLU58 |
| B | THR59 |
| B | ASP130 |
| B | GLU155 |
| B | ASP189 |
| B | HIS300 |
| B | LEU343 |
| B | LEU346 |
| B | HIS352 |
| B | MET357 |
| site_id | AC5 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD C 432 |
| Chain | Residue |
| C | HOH438 |
| D | GLN412 |
| D | LYS425 |
| D | TYR429 |
| C | THR157 |
| C | ASP189 |
| C | ASN190 |
| C | GLY219 |
| C | GLY221 |
| C | ASP222 |
| C | VAL223 |
| C | THR241 |
| C | GLU242 |
| C | ILE243 |
| C | ASP244 |
| C | ASN247 |
| C | THR274 |
| C | THR275 |
| C | GLY276 |
| C | CYS277 |
| C | ILE280 |
| C | ILE298 |
| C | GLY299 |
| C | HIS300 |
| C | LEU343 |
| C | ASN345 |
| C | HIS352 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADN C 433 |
| Chain | Residue |
| C | HIS54 |
| C | THR56 |
| C | GLU58 |
| C | ASP130 |
| C | GLU155 |
| C | ASP189 |
| C | HIS300 |
| C | LEU343 |
| C | LEU346 |
| C | HIS352 |
| C | MET357 |
| site_id | AC7 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD D 432 |
| Chain | Residue |
| C | GLN412 |
| C | LYS425 |
| C | TYR429 |
| D | THR157 |
| D | ASP189 |
| D | ASN190 |
| D | GLY219 |
| D | GLY221 |
| D | ASP222 |
| D | VAL223 |
| D | THR241 |
| D | GLU242 |
| D | ILE243 |
| D | ASP244 |
| D | ASN247 |
| D | THR274 |
| D | THR275 |
| D | GLY276 |
| D | CYS277 |
| D | ILE280 |
| D | ILE298 |
| D | GLY299 |
| D | HIS300 |
| D | LEU343 |
| D | ASN345 |
| D | HIS352 |
| D | HOH435 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADN D 433 |
| Chain | Residue |
| D | HIS54 |
| D | THR56 |
| D | GLU58 |
| D | ASP130 |
| D | GLU155 |
| D | ASP189 |
| D | LEU343 |
| D | LEU346 |
| D | GLY351 |
| D | HIS352 |
| D | MET357 |
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 | SER77-ILE91 |
| site_id | PS00739 |
| Number of Residues | 17 |
| Details | ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKvavVaGYGdVGKGc.A |
| Chain | Residue | Details |
| A | GLY212-ALA228 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11741948 |
| Chain | Residue | Details |
| A | VAL57 | |
| A | THR156 | |
| B | VAL57 | |
| B | THR156 | |
| C | VAL57 | |
| C | THR156 | |
| D | VAL57 | |
| D | THR156 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11927587 |
| Chain | Residue | Details |
| A | GLY131 | |
| B | GLY131 | |
| C | GLY131 | |
| D | GLY131 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10913437, ECO:0000269|PubMed:11741948, ECO:0000269|PubMed:11927587, ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U, ECO:0007744|PDB:1KY5, ECO:0007744|PDB:2H5L |
| Chain | Residue | Details |
| A | THR157 | |
| B | THR157 | |
| C | THR157 | |
| D | THR157 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11741948, ECO:0000269|PubMed:11927587 |
| Chain | Residue | Details |
| A | SER186 | |
| A | ASN190 | |
| B | SER186 | |
| B | ASN190 | |
| C | SER186 | |
| C | ASN190 | |
| D | SER186 | |
| D | ASN190 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10387078 |
| Chain | Residue | Details |
| A | ASP222 | |
| A | ILE243 | |
| B | ASP222 | |
| B | ILE243 | |
| C | ASP222 | |
| C | ILE243 | |
| D | ASP222 | |
| D | ILE243 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10913437, ECO:0000269|PubMed:11741948, ECO:0000269|PubMed:11927587, ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U, ECO:0007744|PDB:1KY4, ECO:0007744|PDB:1XWF, ECO:0007744|PDB:2H5L |
| Chain | Residue | Details |
| A | ALA248 | |
| B | ALA248 | |
| C | ALA248 | |
| D | ALA248 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10387078, ECO:0000269|PubMed:10913437, ECO:0000269|PubMed:11741948, ECO:0000269|PubMed:11927587, ECO:0007744|PDB:1B3R, ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U, ECO:0007744|PDB:1KY4, ECO:0007744|PDB:1KY5, ECO:0007744|PDB:1XWF, ECO:0007744|PDB:2H5L |
| Chain | Residue | Details |
| A | GLY299 | |
| D | GLY299 | |
| D | LEU346 | |
| D | ARG430 | |
| A | LEU346 | |
| A | ARG430 | |
| B | GLY299 | |
| B | LEU346 | |
| B | ARG430 | |
| C | GLY299 | |
| C | LEU346 | |
| C | ARG430 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10387078, ECO:0000269|PubMed:10913437, ECO:0000269|PubMed:11741948, ECO:0007744|PDB:1B3R, ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U, ECO:0007744|PDB:1XWF, ECO:0007744|PDB:2H5L |
| Chain | Residue | Details |
| A | PRO353 | |
| B | PRO353 | |
| C | PRO353 | |
| D | PRO353 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10387078, ECO:0000269|PubMed:11741948, ECO:0000269|PubMed:11927587, ECO:0007744|PDB:1B3R, ECO:0007744|PDB:1K0U, ECO:0007744|PDB:1KY4, ECO:0007744|PDB:1KY5, ECO:0007744|PDB:1XWF, ECO:0007744|PDB:2H5L |
| Chain | Residue | Details |
| A | PRO426 | |
| B | PRO426 | |
| C | PRO426 | |
| D | PRO426 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P23526 |
| Chain | Residue | Details |
| A | VAL183 | |
| B | VAL183 | |
| C | VAL183 | |
| D | VAL183 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P23526 |
| Chain | Residue | Details |
| A | SER186 | |
| B | SER186 | |
| C | SER186 | |
| D | SER186 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P50247 |
| Chain | Residue | Details |
| A | GLY193 | |
| B | GLY193 | |
| C | GLY193 | |
| D | GLY193 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| A | HIS54 | |
| A | ASN185 | |
| A | ASP189 | |
| A | HIS300 | |
| A | ASP130 | |
| A | CYS194 | |
| A | ASN190 |
| site_id | CSA2 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| B | HIS54 | |
| B | ASN185 | |
| B | ASP189 | |
| B | HIS300 | |
| B | ASP130 | |
| B | CYS194 | |
| B | ASN190 |
| site_id | CSA3 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| C | HIS54 | |
| C | ASN185 | |
| C | ASP189 | |
| C | HIS300 | |
| C | ASP130 | |
| C | CYS194 | |
| C | ASN190 |
| site_id | CSA4 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| D | HIS54 | |
| D | ASN185 | |
| D | ASP189 | |
| D | HIS300 | |
| D | ASP130 | |
| D | CYS194 | |
| D | ASN190 |
| site_id | MCSA1 |
| Number of Residues | 14 |
| Details | M-CSA 90 |
| Chain | Residue | Details |
| A | MET55 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| A | ARG195 | electrostatic stabiliser, polar/non-polar interaction |
| A | PHE301 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | PRO353 | electrostatic stabiliser |
| A | PHE361 | electrostatic stabiliser, hydrogen bond donor |
| A | VAL365 | activator, electrostatic stabiliser |
| A | CYS78 | electrostatic stabiliser |
| A | THR83 | electrostatic stabiliser |
| A | GLY131 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| A | THR156 | electrostatic stabiliser, proton acceptor, proton donor |
| A | ASP181 | activator, electrostatic stabiliser |
| A | SER186 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASN190 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| A | LEU191 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA2 |
| Number of Residues | 14 |
| Details | M-CSA 90 |
| Chain | Residue | Details |
| B | MET55 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| B | ARG195 | electrostatic stabiliser, polar/non-polar interaction |
| B | PHE301 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| B | PRO353 | electrostatic stabiliser |
| B | PHE361 | electrostatic stabiliser, hydrogen bond donor |
| B | VAL365 | activator, electrostatic stabiliser |
| B | CYS78 | electrostatic stabiliser |
| B | THR83 | electrostatic stabiliser |
| B | GLY131 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| B | THR156 | electrostatic stabiliser, proton acceptor, proton donor |
| B | ASP181 | activator, electrostatic stabiliser |
| B | SER186 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASN190 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| B | LEU191 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA3 |
| Number of Residues | 14 |
| Details | M-CSA 90 |
| Chain | Residue | Details |
| C | MET55 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| C | ARG195 | electrostatic stabiliser, polar/non-polar interaction |
| C | PHE301 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| C | PRO353 | electrostatic stabiliser |
| C | PHE361 | electrostatic stabiliser, hydrogen bond donor |
| C | VAL365 | activator, electrostatic stabiliser |
| C | CYS78 | electrostatic stabiliser |
| C | THR83 | electrostatic stabiliser |
| C | GLY131 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| C | THR156 | electrostatic stabiliser, proton acceptor, proton donor |
| C | ASP181 | activator, electrostatic stabiliser |
| C | SER186 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | ASN190 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| C | LEU191 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA4 |
| Number of Residues | 14 |
| Details | M-CSA 90 |
| Chain | Residue | Details |
| D | MET55 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| D | ARG195 | electrostatic stabiliser, polar/non-polar interaction |
| D | PHE301 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| D | PRO353 | electrostatic stabiliser |
| D | PHE361 | electrostatic stabiliser, hydrogen bond donor |
| D | VAL365 | activator, electrostatic stabiliser |
| D | CYS78 | electrostatic stabiliser |
| D | THR83 | electrostatic stabiliser |
| D | GLY131 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| D | THR156 | electrostatic stabiliser, proton acceptor, proton donor |
| D | ASP181 | activator, electrostatic stabiliser |
| D | SER186 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | ASN190 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| D | LEU191 | electrostatic stabiliser, hydrogen bond acceptor |
