8QNO
Crystal structure of S-adenosyl-L-homocysteine hydrolase treated at 368 K from Pyrococcus furiosus in complex with inosine
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 |
A | 0071269 | biological_process | L-homocysteine biosynthetic process |
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 |
B | 0071269 | biological_process | L-homocysteine biosynthetic process |
Functional Information from PROSITE/UniProt
site_id | PS00738 |
Number of Residues | 15 |
Details | ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. ASNpLSTQDdVVAAL |
Chain | Residue | Details |
A | ALA78-LEU92 |
site_id | PS00739 |
Number of Residues | 17 |
Details | ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKnvvVvGYGwCGRGi.A |
Chain | Residue | Details |
A | GLY210-ALA226 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 22 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00563 |
Chain | Residue | Details |
A | ASP128 | |
A | ALA296 | |
A | ASN343 | |
B | ASP128 | |
B | GLU153 | |
B | THR154 | |
B | LYS183 | |
B | ASP187 | |
B | ASN188 | |
B | GLY217 | |
B | GLU240 | |
A | GLU153 | |
B | ASN275 | |
B | ALA296 | |
B | ASN343 | |
A | THR154 | |
A | LYS183 | |
A | ASP187 | |
A | ASN188 | |
A | GLY217 | |
A | GLU240 | |
A | ASN275 |