3G1U
Crystal structure of Leishmania major S-adenosylhomocysteine hydrolase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004013 | molecular_function | adenosylhomocysteinase activity |
| A | 0005737 | cellular_component | cytoplasm |
| 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004013 | molecular_function | adenosylhomocysteinase activity |
| B | 0005737 | cellular_component | cytoplasm |
| 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004013 | molecular_function | adenosylhomocysteinase activity |
| C | 0005737 | cellular_component | cytoplasm |
| 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 |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004013 | molecular_function | adenosylhomocysteinase activity |
| D | 0005737 | cellular_component | cytoplasm |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADN A 438 |
| Chain | Residue |
| A | LEU51 |
| A | LEU343 |
| A | SER350 |
| A | HIS352 |
| A | MET357 |
| A | NAD439 |
| A | HOH663 |
| A | HIS52 |
| A | THR54 |
| A | GLN56 |
| A | THR57 |
| A | ASP130 |
| A | GLU155 |
| A | THR156 |
| A | HIS300 |
| site_id | AC2 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD A 439 |
| Chain | Residue |
| A | THR156 |
| A | THR157 |
| A | THR158 |
| A | ASN190 |
| A | GLY219 |
| A | GLY221 |
| A | ASP222 |
| A | VAL223 |
| A | THR241 |
| A | GLU242 |
| A | VAL243 |
| A | ASP244 |
| A | ASN247 |
| A | THR274 |
| A | THR275 |
| A | GLY276 |
| A | ILE280 |
| A | ILE298 |
| A | GLY299 |
| A | HIS300 |
| A | LEU343 |
| A | ASN345 |
| A | HIS352 |
| A | ADN438 |
| A | HOH450 |
| A | HOH453 |
| A | HOH524 |
| A | HOH562 |
| A | HOH664 |
| A | HOH671 |
| A | HOH672 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADN B 438 |
| Chain | Residue |
| B | LEU51 |
| B | HIS52 |
| B | THR54 |
| B | GLN56 |
| B | THR57 |
| B | ASP130 |
| B | GLU155 |
| B | THR156 |
| B | HIS300 |
| B | SER350 |
| B | HIS352 |
| B | MET357 |
| B | NAD439 |
| B | HOH537 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD B 439 |
| Chain | Residue |
| B | THR156 |
| B | THR157 |
| B | THR158 |
| B | LYS161 |
| B | ASN190 |
| B | GLY219 |
| B | GLY221 |
| B | ASP222 |
| B | VAL223 |
| B | THR241 |
| B | GLU242 |
| B | VAL243 |
| B | ASP244 |
| B | ASN247 |
| B | THR274 |
| B | THR275 |
| B | GLY276 |
| B | ASN277 |
| B | ILE280 |
| B | ILE298 |
| B | GLY299 |
| B | HIS300 |
| B | LEU343 |
| B | ASN345 |
| B | HIS352 |
| B | ADN438 |
| B | HOH461 |
| B | HOH486 |
| B | HOH540 |
| C | GLN418 |
| C | LYS431 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADN C 438 |
| Chain | Residue |
| C | ASP189 |
| C | HIS300 |
| C | SER350 |
| C | HIS352 |
| C | MET357 |
| C | NAD439 |
| C | HIS52 |
| C | THR54 |
| C | GLN56 |
| C | THR57 |
| C | ASP130 |
| C | GLU155 |
| C | THR156 |
| C | LYS185 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD C 439 |
| Chain | Residue |
| C | THR156 |
| C | THR157 |
| C | THR158 |
| C | ASN190 |
| C | GLY219 |
| C | GLY221 |
| C | ASP222 |
| C | VAL223 |
| C | THR241 |
| C | GLU242 |
| C | VAL243 |
| C | ASP244 |
| C | ASN247 |
| C | THR274 |
| C | THR275 |
| C | GLY276 |
| C | ILE280 |
| C | ILE298 |
| C | GLY299 |
| C | HIS300 |
| C | ASN345 |
| C | HIS352 |
| C | ADN438 |
| C | HOH444 |
| C | HOH478 |
| C | HOH517 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADN D 438 |
| Chain | Residue |
| D | LEU51 |
| D | HIS52 |
| D | THR54 |
| D | GLN56 |
| D | THR57 |
| D | ASP130 |
| D | GLU155 |
| D | THR156 |
| D | ASP189 |
| D | HIS300 |
| D | LEU343 |
| D | SER350 |
| D | HIS352 |
| D | MET357 |
| D | PHE361 |
| D | NAD439 |
| site_id | AC8 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD D 439 |
| Chain | Residue |
| D | THR156 |
| D | THR157 |
| D | THR158 |
| D | LYS161 |
| D | ASP189 |
| D | ASN190 |
| D | GLY219 |
| D | GLY221 |
| D | ASP222 |
| D | VAL223 |
| D | THR241 |
| D | GLU242 |
| D | VAL243 |
| D | ASP244 |
| D | ASN247 |
| D | THR274 |
| D | THR275 |
| D | GLY276 |
| D | ASN277 |
| D | ILE280 |
| D | ILE298 |
| D | GLY299 |
| D | HIS300 |
| D | ASN345 |
| D | HIS352 |
| D | ADN438 |
| D | HOH456 |
| D | HOH471 |
| D | HOH486 |
| D | HOH510 |
| D | HOH700 |
Functional Information from PROSITE/UniProt
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CvCgyGdvGKgC |
| Chain | Residue | Details |
| A | CYS216-CYS227 |
| site_id | PS00738 |
| Number of Residues | 15 |
| Details | ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiFSTQDnAAAAI |
| Chain | Residue | Details |
| A | SER75-ILE89 |
| site_id | PS00739 |
| Number of Residues | 18 |
| Details | ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKtccVcGYGdVGKGcaA |
| Chain | Residue | Details |
| A | GLY212-ALA229 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| A | HIS300 | |
| A | ASP189 | |
| A | HIS52 | |
| A | ASP130 | |
| A | CYS194 | |
| A | ASN190 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| B | HIS300 | |
| B | ASP189 | |
| B | HIS52 | |
| 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 | LYS185 | |
| C | ASP189 | |
| C | HIS300 | |
| C | HIS52 | |
| C | ASP130 | |
| C | CYS194 | |
| C | ASN190 |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| D | HIS300 | |
| D | ASP189 | |
| D | HIS52 | |
| D | ASP130 | |
| D | CYS194 | |
| D | ASN190 |
