1K0U
Inhibition of S-adenosylhomocysteine Hydrolase by "acyclic sugar" Adenosine Analogue D-eritadenine
Replaces: 1D4GFunctional 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 | 0033528 | biological_process | S-methylmethionine 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 | 0033528 | biological_process | S-methylmethionine 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 | 0033528 | biological_process | S-methylmethionine 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 | 0033528 | biological_process | S-methylmethionine 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 |
| E | 0001666 | biological_process | response to hypoxia |
| E | 0002439 | biological_process | chronic inflammatory response to antigenic stimulus |
| E | 0004013 | molecular_function | adenosylhomocysteinase activity |
| E | 0005507 | molecular_function | copper ion 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 | 0007584 | biological_process | response to nutrient |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0019510 | biological_process | S-adenosylhomocysteine catabolic process |
| E | 0030554 | molecular_function | adenyl nucleotide binding |
| E | 0033353 | biological_process | S-adenosylmethionine cycle |
| E | 0033528 | biological_process | S-methylmethionine cycle |
| E | 0042470 | cellular_component | melanosome |
| E | 0042745 | biological_process | circadian sleep/wake cycle |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0051287 | molecular_function | NAD binding |
| E | 0098604 | molecular_function | adenosylselenohomocysteinase activity |
| F | 0001666 | biological_process | response to hypoxia |
| F | 0002439 | biological_process | chronic inflammatory response to antigenic stimulus |
| F | 0004013 | molecular_function | adenosylhomocysteinase activity |
| F | 0005507 | molecular_function | copper ion 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 | 0007584 | biological_process | response to nutrient |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0019510 | biological_process | S-adenosylhomocysteine catabolic process |
| F | 0030554 | molecular_function | adenyl nucleotide binding |
| F | 0033353 | biological_process | S-adenosylmethionine cycle |
| F | 0033528 | biological_process | S-methylmethionine cycle |
| F | 0042470 | cellular_component | melanosome |
| F | 0042745 | biological_process | circadian sleep/wake cycle |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0051287 | molecular_function | NAD binding |
| F | 0098604 | molecular_function | adenosylselenohomocysteinase activity |
| G | 0001666 | biological_process | response to hypoxia |
| G | 0002439 | biological_process | chronic inflammatory response to antigenic stimulus |
| G | 0004013 | molecular_function | adenosylhomocysteinase activity |
| G | 0005507 | molecular_function | copper ion binding |
| G | 0005634 | cellular_component | nucleus |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005783 | cellular_component | endoplasmic reticulum |
| G | 0005829 | cellular_component | cytosol |
| G | 0006730 | biological_process | one-carbon metabolic process |
| G | 0007584 | biological_process | response to nutrient |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0019510 | biological_process | S-adenosylhomocysteine catabolic process |
| G | 0030554 | molecular_function | adenyl nucleotide binding |
| G | 0033353 | biological_process | S-adenosylmethionine cycle |
| G | 0033528 | biological_process | S-methylmethionine cycle |
| G | 0042470 | cellular_component | melanosome |
| G | 0042745 | biological_process | circadian sleep/wake cycle |
| G | 0042802 | molecular_function | identical protein binding |
| G | 0051287 | molecular_function | NAD binding |
| G | 0098604 | molecular_function | adenosylselenohomocysteinase activity |
| H | 0001666 | biological_process | response to hypoxia |
| H | 0002439 | biological_process | chronic inflammatory response to antigenic stimulus |
| H | 0004013 | molecular_function | adenosylhomocysteinase activity |
| H | 0005507 | molecular_function | copper ion binding |
| H | 0005634 | cellular_component | nucleus |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005783 | cellular_component | endoplasmic reticulum |
| H | 0005829 | cellular_component | cytosol |
| H | 0006730 | biological_process | one-carbon metabolic process |
| H | 0007584 | biological_process | response to nutrient |
| H | 0016787 | molecular_function | hydrolase activity |
| H | 0019510 | biological_process | S-adenosylhomocysteine catabolic process |
| H | 0030554 | molecular_function | adenyl nucleotide binding |
| H | 0033353 | biological_process | S-adenosylmethionine cycle |
| H | 0033528 | biological_process | S-methylmethionine cycle |
| H | 0042470 | cellular_component | melanosome |
| H | 0042745 | biological_process | circadian sleep/wake cycle |
| H | 0042802 | molecular_function | identical protein binding |
| H | 0051287 | molecular_function | NAD binding |
| H | 0098604 | molecular_function | adenosylselenohomocysteinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD A 1432 |
| Chain | Residue |
| A | THR156 |
| A | GLU242 |
| A | ILE243 |
| A | ASP244 |
| A | ASN247 |
| A | THR274 |
| A | THR275 |
| A | ILE280 |
| A | ILE298 |
| A | GLY299 |
| A | HIS300 |
| A | THR157 |
| A | LEU343 |
| A | ASN345 |
| A | HIS352 |
| A | DEA1433 |
| A | HOH9224 |
| B | GLN412 |
| B | LYS425 |
| B | TYR429 |
| A | THR158 |
| A | ASN190 |
| A | GLY219 |
| A | GLY221 |
| A | ASP222 |
| A | VAL223 |
| A | THR241 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DEA A 1433 |
| Chain | Residue |
| A | HIS54 |
| A | THR56 |
| A | GLU58 |
| A | THR59 |
| A | ASP130 |
| A | GLU155 |
| A | THR156 |
| A | LYS185 |
| A | ASP189 |
| A | LEU346 |
| A | GLY351 |
| A | HIS352 |
| A | PHE361 |
| A | NAD1432 |
| site_id | AC3 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD B 2432 |
| Chain | Residue |
| A | GLN412 |
| A | LYS425 |
| A | TYR429 |
| B | THR156 |
| B | THR157 |
| B | THR158 |
| B | ASN190 |
| B | GLY219 |
| B | GLY221 |
| B | ASP222 |
| B | VAL223 |
| B | THR241 |
| B | GLU242 |
| B | ILE243 |
| B | ASP244 |
| B | ASN247 |
| B | THR274 |
| B | THR275 |
| B | ILE280 |
| B | ILE298 |
| B | GLY299 |
| B | HIS300 |
| B | LEU343 |
| B | ASN345 |
| B | HIS352 |
| B | DEA2433 |
| B | HOH9363 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DEA B 2433 |
| Chain | Residue |
| B | HIS54 |
| B | THR56 |
| B | GLU58 |
| B | THR59 |
| B | ASP130 |
| B | GLU155 |
| B | THR156 |
| B | LYS185 |
| B | ASP189 |
| B | LEU346 |
| B | GLY351 |
| B | HIS352 |
| B | PHE361 |
| B | NAD2432 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD C 3432 |
| Chain | Residue |
| C | GLY299 |
| C | HIS300 |
| C | LEU343 |
| C | ASN345 |
| C | HIS352 |
| C | DEA3433 |
| D | GLN412 |
| D | LYS425 |
| D | TYR429 |
| C | THR156 |
| C | THR157 |
| C | THR158 |
| 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 | ILE280 |
| C | ILE298 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE DEA C 3433 |
| Chain | Residue |
| C | HIS54 |
| C | THR56 |
| C | GLU58 |
| C | THR59 |
| C | ASP130 |
| C | GLU155 |
| C | THR156 |
| C | LYS185 |
| C | ASP189 |
| C | LEU346 |
| C | GLY351 |
| C | HIS352 |
| C | MET357 |
| C | PHE361 |
| C | NAD3432 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD D 4432 |
| Chain | Residue |
| C | GLN412 |
| C | LYS425 |
| C | TYR429 |
| D | THR156 |
| D | THR157 |
| D | THR158 |
| 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 | ILE280 |
| D | ILE298 |
| D | GLY299 |
| D | HIS300 |
| D | LEU343 |
| D | ASN345 |
| D | HIS352 |
| D | DEA4433 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE DEA D 4433 |
| Chain | Residue |
| D | HIS54 |
| D | THR56 |
| D | GLU58 |
| D | THR59 |
| D | ASP130 |
| D | GLU155 |
| D | THR156 |
| D | LYS185 |
| D | ASP189 |
| D | LEU346 |
| D | GLY351 |
| D | HIS352 |
| D | MET357 |
| D | PHE361 |
| D | NAD4432 |
| site_id | AC9 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD E 5432 |
| Chain | Residue |
| E | THR156 |
| E | THR157 |
| E | THR158 |
| E | ASN190 |
| E | GLY219 |
| E | GLY221 |
| E | ASP222 |
| E | VAL223 |
| E | THR241 |
| E | GLU242 |
| E | ILE243 |
| E | ASP244 |
| E | ASN247 |
| E | THR274 |
| E | THR275 |
| E | ILE280 |
| E | ILE298 |
| E | GLY299 |
| E | HIS300 |
| E | LEU343 |
| E | ASN345 |
| E | HIS352 |
| E | DEA5433 |
| E | HOH9406 |
| F | GLN412 |
| F | LYS425 |
| F | TYR429 |
| site_id | BC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE DEA E 5433 |
| Chain | Residue |
| E | LEU53 |
| E | HIS54 |
| E | THR56 |
| E | GLU58 |
| E | THR59 |
| E | ASP130 |
| E | GLU155 |
| E | THR156 |
| E | ASN180 |
| E | LYS185 |
| E | ASP189 |
| E | ASN345 |
| E | LEU346 |
| E | GLY351 |
| E | HIS352 |
| E | MET357 |
| E | PHE361 |
| E | NAD5432 |
| site_id | BC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD F 6432 |
| Chain | Residue |
| E | LEU408 |
| E | GLN412 |
| E | LYS425 |
| E | TYR429 |
| F | THR156 |
| F | THR157 |
| F | THR158 |
| F | ASN190 |
| F | GLY219 |
| F | GLY221 |
| F | ASP222 |
| F | VAL223 |
| F | THR241 |
| F | GLU242 |
| F | ILE243 |
| F | ASP244 |
| F | ASN247 |
| F | THR274 |
| F | THR275 |
| F | CYS277 |
| F | ILE280 |
| F | ILE298 |
| F | GLY299 |
| F | HIS300 |
| F | LEU343 |
| F | ASN345 |
| F | HIS352 |
| F | DEA6433 |
| site_id | BC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE DEA F 6433 |
| Chain | Residue |
| F | HIS54 |
| F | THR56 |
| F | GLU58 |
| F | THR59 |
| F | ASP130 |
| F | GLU155 |
| F | THR156 |
| F | ASN180 |
| F | LYS185 |
| F | ASP189 |
| F | LEU346 |
| F | GLY351 |
| F | HIS352 |
| F | MET357 |
| F | NAD6432 |
| F | HOH9309 |
| site_id | BC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD G 7432 |
| Chain | Residue |
| G | THR156 |
| G | THR157 |
| G | THR158 |
| G | ASN190 |
| G | GLY219 |
| G | GLY221 |
| G | ASP222 |
| G | VAL223 |
| G | THR241 |
| G | GLU242 |
| G | ILE243 |
| G | ASP244 |
| G | ASN247 |
| G | THR274 |
| G | THR275 |
| G | ILE280 |
| G | ILE298 |
| G | GLY299 |
| G | HIS300 |
| G | LEU343 |
| G | ASN345 |
| G | HIS352 |
| G | DEA7433 |
| H | LYS425 |
| H | TYR429 |
| site_id | BC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE DEA G 7433 |
| Chain | Residue |
| G | HIS54 |
| G | THR56 |
| G | GLU58 |
| G | THR59 |
| G | ASP130 |
| G | GLU155 |
| G | THR156 |
| G | LYS185 |
| G | ASP189 |
| G | ASN345 |
| G | LEU346 |
| G | MET350 |
| G | GLY351 |
| G | HIS352 |
| G | MET357 |
| G | NAD7432 |
| site_id | BC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD H 8432 |
| Chain | Residue |
| G | GLN412 |
| G | LYS425 |
| G | TYR429 |
| H | THR156 |
| H | THR157 |
| H | THR158 |
| H | ASN190 |
| H | GLY219 |
| H | GLY221 |
| H | ASP222 |
| H | VAL223 |
| H | THR241 |
| H | GLU242 |
| H | ILE243 |
| H | ASP244 |
| H | ASN247 |
| H | THR274 |
| H | THR275 |
| H | ILE280 |
| H | ILE298 |
| H | GLY299 |
| H | HIS300 |
| H | LEU343 |
| H | ASN345 |
| H | DEA8433 |
| H | HOH9255 |
| site_id | BC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE DEA H 8433 |
| Chain | Residue |
| H | LEU53 |
| H | THR56 |
| H | GLU58 |
| H | THR59 |
| H | ASP130 |
| H | GLU155 |
| H | THR156 |
| H | ASN180 |
| H | LYS185 |
| H | ASP189 |
| H | ASN190 |
| H | LEU346 |
| H | HIS352 |
| H | MET357 |
| H | NAD8432 |
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 | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11741948 |
| Chain | Residue | Details |
| A | VAL57 | |
| E | THR156 | |
| F | VAL57 | |
| F | THR156 | |
| G | VAL57 | |
| G | THR156 | |
| H | VAL57 | |
| H | THR156 | |
| A | THR156 | |
| B | VAL57 | |
| B | THR156 | |
| C | VAL57 | |
| C | THR156 | |
| D | VAL57 | |
| D | THR156 | |
| E | VAL57 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11927587 |
| Chain | Residue | Details |
| A | GLY131 | |
| B | GLY131 | |
| C | GLY131 | |
| D | GLY131 | |
| E | GLY131 | |
| F | GLY131 | |
| G | GLY131 | |
| H | GLY131 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| 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 | |
| E | THR157 | |
| F | THR157 | |
| G | THR157 | |
| H | THR157 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11741948, ECO:0000269|PubMed:11927587 |
| Chain | Residue | Details |
| A | SER186 | |
| E | ASN190 | |
| F | SER186 | |
| F | ASN190 | |
| G | SER186 | |
| G | ASN190 | |
| H | SER186 | |
| H | ASN190 | |
| A | ASN190 | |
| B | SER186 | |
| B | ASN190 | |
| C | SER186 | |
| C | ASN190 | |
| D | SER186 | |
| D | ASN190 | |
| E | SER186 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10387078 |
| Chain | Residue | Details |
| A | ASP222 | |
| E | ILE243 | |
| F | ASP222 | |
| F | ILE243 | |
| G | ASP222 | |
| G | ILE243 | |
| H | ASP222 | |
| H | ILE243 | |
| A | ILE243 | |
| B | ASP222 | |
| B | ILE243 | |
| C | ASP222 | |
| C | ILE243 | |
| D | ASP222 | |
| D | ILE243 | |
| E | ASP222 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| 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 | |
| E | ALA248 | |
| F | ALA248 | |
| G | ALA248 | |
| H | ALA248 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 24 |
| 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 | |
| E | GLY299 | |
| E | LEU346 | |
| E | ARG430 | |
| F | GLY299 | |
| F | LEU346 | |
| F | ARG430 | |
| G | GLY299 | |
| A | LEU346 | |
| G | LEU346 | |
| G | ARG430 | |
| H | GLY299 | |
| H | LEU346 | |
| H | ARG430 | |
| A | ARG430 | |
| B | GLY299 | |
| B | LEU346 | |
| B | ARG430 | |
| C | GLY299 | |
| C | LEU346 | |
| C | ARG430 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| 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 | |
| E | PRO353 | |
| F | PRO353 | |
| G | PRO353 | |
| H | PRO353 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| 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 | |
| E | PRO426 | |
| F | PRO426 | |
| G | PRO426 | |
| H | PRO426 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P23526 |
| Chain | Residue | Details |
| A | VAL183 | |
| B | VAL183 | |
| C | VAL183 | |
| D | VAL183 | |
| E | VAL183 | |
| F | VAL183 | |
| G | VAL183 | |
| H | VAL183 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P23526 |
| Chain | Residue | Details |
| A | SER186 | |
| B | SER186 | |
| C | SER186 | |
| D | SER186 | |
| E | SER186 | |
| F | SER186 | |
| G | SER186 | |
| H | SER186 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P50247 |
| Chain | Residue | Details |
| A | GLY193 | |
| B | GLY193 | |
| C | GLY193 | |
| D | GLY193 | |
| E | GLY193 | |
| F | GLY193 | |
| G | GLY193 | |
| H | 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 | LYS185 | |
| 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 | LYS185 | |
| 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 | LYS185 | |
| 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 | LYS185 | |
| D | ASP189 | |
| D | HIS300 | |
| D | ASP130 | |
| D | CYS194 | |
| D | ASN190 |
| site_id | CSA5 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| E | HIS54 | |
| E | LYS185 | |
| E | ASP189 | |
| E | HIS300 | |
| E | ASP130 | |
| E | CYS194 | |
| E | ASN190 |
| site_id | CSA6 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| F | HIS54 | |
| F | LYS185 | |
| F | ASP189 | |
| F | HIS300 | |
| F | ASP130 | |
| F | CYS194 | |
| F | ASN190 |
| site_id | CSA7 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| G | HIS54 | |
| G | LYS185 | |
| G | ASP189 | |
| G | HIS300 | |
| G | ASP130 | |
| G | CYS194 | |
| G | ASN190 |
| site_id | CSA8 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| H | HIS54 | |
| H | LYS185 | |
| H | ASP189 | |
| H | HIS300 | |
| H | ASP130 | |
| H | CYS194 | |
| H | ASN190 |
| site_id | MCSA1 |
| Number of Residues | 14 |
| Details | M-CSA 90 |
| Chain | Residue | Details |
| A | HIS54 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| A | CYS194 | electrostatic stabiliser, polar/non-polar interaction |
| A | HIS300 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | HIS352 | electrostatic stabiliser |
| A | SER360 | electrostatic stabiliser, hydrogen bond donor |
| A | GLN364 | activator, electrostatic stabiliser |
| A | SER77 | electrostatic stabiliser |
| A | SER82 | electrostatic stabiliser |
| A | ASP130 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| A | GLU155 | electrostatic stabiliser, proton acceptor, proton donor |
| A | ASN180 | activator, electrostatic stabiliser |
| A | LYS185 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASP189 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| A | ASN190 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA2 |
| Number of Residues | 14 |
| Details | M-CSA 90 |
| Chain | Residue | Details |
| B | HIS54 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| B | CYS194 | electrostatic stabiliser, polar/non-polar interaction |
| B | HIS300 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| B | HIS352 | electrostatic stabiliser |
| B | SER360 | electrostatic stabiliser, hydrogen bond donor |
| B | GLN364 | activator, electrostatic stabiliser |
| B | SER77 | electrostatic stabiliser |
| B | SER82 | electrostatic stabiliser |
| B | ASP130 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| B | GLU155 | electrostatic stabiliser, proton acceptor, proton donor |
| B | ASN180 | activator, electrostatic stabiliser |
| B | LYS185 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASP189 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| B | ASN190 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA3 |
| Number of Residues | 14 |
| Details | M-CSA 90 |
| Chain | Residue | Details |
| C | HIS54 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| C | CYS194 | electrostatic stabiliser, polar/non-polar interaction |
| C | HIS300 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| C | HIS352 | electrostatic stabiliser |
| C | SER360 | electrostatic stabiliser, hydrogen bond donor |
| C | GLN364 | activator, electrostatic stabiliser |
| C | SER77 | electrostatic stabiliser |
| C | SER82 | electrostatic stabiliser |
| C | ASP130 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| C | GLU155 | electrostatic stabiliser, proton acceptor, proton donor |
| C | ASN180 | activator, electrostatic stabiliser |
| C | LYS185 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | ASP189 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| C | ASN190 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA4 |
| Number of Residues | 14 |
| Details | M-CSA 90 |
| Chain | Residue | Details |
| D | HIS54 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| D | CYS194 | electrostatic stabiliser, polar/non-polar interaction |
| D | HIS300 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| D | HIS352 | electrostatic stabiliser |
| D | SER360 | electrostatic stabiliser, hydrogen bond donor |
| D | GLN364 | activator, electrostatic stabiliser |
| D | SER77 | electrostatic stabiliser |
| D | SER82 | electrostatic stabiliser |
| D | ASP130 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| D | GLU155 | electrostatic stabiliser, proton acceptor, proton donor |
| D | ASN180 | activator, electrostatic stabiliser |
| D | LYS185 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | ASP189 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| D | ASN190 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA5 |
| Number of Residues | 14 |
| Details | M-CSA 90 |
| Chain | Residue | Details |
| E | HIS54 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| E | CYS194 | electrostatic stabiliser, polar/non-polar interaction |
| E | HIS300 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| E | HIS352 | electrostatic stabiliser |
| E | SER360 | electrostatic stabiliser, hydrogen bond donor |
| E | GLN364 | activator, electrostatic stabiliser |
| E | SER77 | electrostatic stabiliser |
| E | SER82 | electrostatic stabiliser |
| E | ASP130 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| E | GLU155 | electrostatic stabiliser, proton acceptor, proton donor |
| E | ASN180 | activator, electrostatic stabiliser |
| E | LYS185 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| E | ASP189 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| E | ASN190 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA6 |
| Number of Residues | 14 |
| Details | M-CSA 90 |
| Chain | Residue | Details |
| F | HIS54 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| F | CYS194 | electrostatic stabiliser, polar/non-polar interaction |
| F | HIS300 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| F | HIS352 | electrostatic stabiliser |
| F | SER360 | electrostatic stabiliser, hydrogen bond donor |
| F | GLN364 | activator, electrostatic stabiliser |
| F | SER77 | electrostatic stabiliser |
| F | SER82 | electrostatic stabiliser |
| F | ASP130 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| F | GLU155 | electrostatic stabiliser, proton acceptor, proton donor |
| F | ASN180 | activator, electrostatic stabiliser |
| F | LYS185 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| F | ASP189 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| F | ASN190 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA7 |
| Number of Residues | 14 |
| Details | M-CSA 90 |
| Chain | Residue | Details |
| G | HIS54 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| G | CYS194 | electrostatic stabiliser, polar/non-polar interaction |
| G | HIS300 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| G | HIS352 | electrostatic stabiliser |
| G | SER360 | electrostatic stabiliser, hydrogen bond donor |
| G | GLN364 | activator, electrostatic stabiliser |
| G | SER77 | electrostatic stabiliser |
| G | SER82 | electrostatic stabiliser |
| G | ASP130 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| G | GLU155 | electrostatic stabiliser, proton acceptor, proton donor |
| G | ASN180 | activator, electrostatic stabiliser |
| G | LYS185 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| G | ASP189 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| G | ASN190 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA8 |
| Number of Residues | 14 |
| Details | M-CSA 90 |
| Chain | Residue | Details |
| H | HIS54 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| H | CYS194 | electrostatic stabiliser, polar/non-polar interaction |
| H | HIS300 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| H | HIS352 | electrostatic stabiliser |
| H | SER360 | electrostatic stabiliser, hydrogen bond donor |
| H | GLN364 | activator, electrostatic stabiliser |
| H | SER77 | electrostatic stabiliser |
| H | SER82 | electrostatic stabiliser |
| H | ASP130 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| H | GLU155 | electrostatic stabiliser, proton acceptor, proton donor |
| H | ASN180 | activator, electrostatic stabiliser |
| H | LYS185 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| H | ASP189 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| H | ASN190 | electrostatic stabiliser, hydrogen bond acceptor |
