1V8B
Crystal structure of a hydrolase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004013 | molecular_function | adenosylhomocysteinase activity |
| 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 | 0004013 | molecular_function | adenosylhomocysteinase activity |
| 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 | 0004013 | molecular_function | adenosylhomocysteinase activity |
| 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 | 0004013 | molecular_function | adenosylhomocysteinase activity |
| 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 | 31 |
| Details | BINDING SITE FOR RESIDUE NAD A 501 |
| Chain | Residue |
| A | THR201 |
| A | GLU287 |
| A | ILE288 |
| A | ASP289 |
| A | CYS292 |
| A | CYS319 |
| A | THR320 |
| A | GLY321 |
| A | ASN322 |
| A | ILE343 |
| A | GLY344 |
| A | THR202 |
| A | HIS345 |
| A | LEU389 |
| A | ASN391 |
| A | HIS398 |
| A | ADN502 |
| A | HOH504 |
| A | HOH523 |
| A | HOH533 |
| A | HOH576 |
| B | GLN460 |
| A | THR203 |
| B | LYS473 |
| B | TYR477 |
| A | ASN235 |
| A | GLY264 |
| A | GLY266 |
| A | ASP267 |
| A | VAL268 |
| A | THR286 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADN A 502 |
| Chain | Residue |
| A | HIS54 |
| A | THR56 |
| A | GLU58 |
| A | ASP134 |
| A | GLU200 |
| A | THR201 |
| A | LYS230 |
| A | ASP234 |
| A | LEU389 |
| A | THR396 |
| A | HIS398 |
| A | MET403 |
| A | NAD501 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD B 501 |
| Chain | Residue |
| A | GLN460 |
| A | LYS473 |
| A | TYR477 |
| B | THR201 |
| B | THR202 |
| B | THR203 |
| B | ASN235 |
| B | GLY264 |
| B | GLY266 |
| B | ASP267 |
| B | VAL268 |
| B | THR286 |
| B | GLU287 |
| B | ILE288 |
| B | ASP289 |
| B | CYS292 |
| B | CYS319 |
| B | THR320 |
| B | GLY321 |
| B | ASN322 |
| B | ILE343 |
| B | GLY344 |
| B | HIS345 |
| B | LEU389 |
| B | ASN391 |
| B | HIS398 |
| B | ADN1502 |
| B | HOH1503 |
| B | HOH1546 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADN B 1502 |
| Chain | Residue |
| B | HIS54 |
| B | THR56 |
| B | GLU58 |
| B | ASP134 |
| B | GLU200 |
| B | THR201 |
| B | LYS230 |
| B | ASP234 |
| B | LEU389 |
| B | THR396 |
| B | HIS398 |
| B | MET403 |
| B | NAD501 |
| B | HOH1537 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD C 501 |
| Chain | Residue |
| C | CYS292 |
| C | CYS319 |
| C | THR320 |
| C | GLY321 |
| C | ASN322 |
| C | ILE343 |
| C | GLY344 |
| C | HIS345 |
| C | LEU389 |
| C | ASN391 |
| C | HIS398 |
| C | ADN2502 |
| C | HOH2519 |
| C | HOH2525 |
| C | HOH2529 |
| C | HOH2536 |
| C | HOH2549 |
| D | GLN460 |
| D | LYS473 |
| D | TYR477 |
| C | THR201 |
| C | THR202 |
| C | THR203 |
| C | ASN235 |
| C | GLY264 |
| C | GLY266 |
| C | ASP267 |
| C | VAL268 |
| C | THR286 |
| C | GLU287 |
| C | ILE288 |
| C | ASP289 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADN C 2502 |
| Chain | Residue |
| C | LEU53 |
| C | HIS54 |
| C | THR56 |
| C | GLU58 |
| C | ASP134 |
| C | GLU200 |
| C | THR201 |
| C | LYS230 |
| C | ASP234 |
| C | LEU389 |
| C | THR396 |
| C | HIS398 |
| C | MET403 |
| C | PHE407 |
| C | NAD501 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD D 501 |
| Chain | Residue |
| C | GLN460 |
| C | LYS473 |
| C | TYR477 |
| D | THR201 |
| D | THR202 |
| D | THR203 |
| D | ASN235 |
| D | GLY264 |
| D | GLY266 |
| D | ASP267 |
| D | VAL268 |
| D | THR286 |
| D | GLU287 |
| D | ILE288 |
| D | ASP289 |
| D | CYS292 |
| D | CYS319 |
| D | THR320 |
| D | GLY321 |
| D | ASN322 |
| D | ILE343 |
| D | GLY344 |
| D | HIS345 |
| D | LEU389 |
| D | ASN391 |
| D | HIS398 |
| D | ADN3502 |
| D | HOH3549 |
| D | HOH3579 |
| D | HOH3597 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADN D 3502 |
| Chain | Residue |
| D | HIS54 |
| D | THR56 |
| D | GLU58 |
| D | ASP134 |
| D | GLU200 |
| D | THR201 |
| D | LYS230 |
| D | ASP234 |
| D | LEU389 |
| D | THR396 |
| D | GLY397 |
| D | HIS398 |
| D | MET403 |
| D | NAD501 |
| D | HOH3547 |
Functional Information from PROSITE/UniProt
| site_id | PS00738 |
| Number of Residues | 15 |
| Details | ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiYSTADyAAAAV |
| Chain | Residue | Details |
| A | SER77-VAL91 |
| site_id | PS00739 |
| Number of Residues | 18 |
| Details | ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKivvIcGYGdVGKGcaS |
| Chain | Residue | Details |
| A | GLY257-SER274 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 52 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15476817","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for nucleoside inhibitor binding"} |
| Chain | Residue | Details |
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 | HIS345 | |
| A | ASP234 | |
| A | ASP134 | |
| A | CYS239 | |
| A | LYS230 | |
| A | ASN235 |
| site_id | CSA2 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| B | HIS54 | |
| B | HIS345 | |
| B | ASP234 | |
| B | ASP134 | |
| B | CYS239 | |
| B | LYS230 | |
| B | ASN235 |
| site_id | CSA3 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| C | HIS54 | |
| C | HIS345 | |
| C | ASP234 | |
| C | ASP134 | |
| C | CYS239 | |
| C | LYS230 | |
| C | ASN235 |
| site_id | CSA4 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| D | HIS54 | |
| D | HIS345 | |
| D | ASP234 | |
| D | ASP134 | |
| D | CYS239 | |
| D | LYS230 | |
| D | ASN235 |
