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 |