Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004013 | molecular_function | adenosylhomocysteinase activity |
| B | 0004013 | molecular_function | adenosylhomocysteinase activity |
| C | 0004013 | molecular_function | adenosylhomocysteinase activity |
| D | 0004013 | molecular_function | adenosylhomocysteinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD A 608 |
| Chain | Residue |
| A | ASP369 |
| A | ASP424 |
| A | CYS427 |
| A | CYS454 |
| A | THR455 |
| A | GLY456 |
| A | ASN457 |
| A | MET478 |
| A | GLY479 |
| A | HIS480 |
| A | ASN525 |
| A | ASN370 |
| A | HOH619 |
| A | HOH621 |
| A | HOH656 |
| A | HOH657 |
| A | HOH745 |
| A | HOH755 |
| A | HOH756 |
| A | HOH763 |
| C | LYS605 |
| A | GLY399 |
| A | GLY401 |
| A | GLU402 |
| A | VAL403 |
| A | THR421 |
| A | GLU422 |
| A | ILE423 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD B 608 |
| Chain | Residue |
| B | ASP369 |
| B | ASN370 |
| B | GLY401 |
| B | GLU402 |
| B | VAL403 |
| B | THR421 |
| B | GLU422 |
| B | ILE423 |
| B | ASP424 |
| B | CYS427 |
| B | CYS454 |
| B | THR455 |
| B | GLY456 |
| B | ASN457 |
| B | MET478 |
| B | GLY479 |
| B | HIS480 |
| B | LEU523 |
| B | ASN525 |
| B | HOH696 |
| B | HOH706 |
| B | HOH709 |
| B | HOH741 |
| B | HOH742 |
| D | LYS605 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD C 608 |
| Chain | Residue |
| A | LYS605 |
| C | ASP369 |
| C | ASN370 |
| C | GLY399 |
| C | GLY401 |
| C | GLU402 |
| C | VAL403 |
| C | THR421 |
| C | GLU422 |
| C | ILE423 |
| C | ASP424 |
| C | CYS427 |
| C | CYS454 |
| C | THR455 |
| C | GLY456 |
| C | ASN457 |
| C | VAL460 |
| C | MET478 |
| C | GLY479 |
| C | HIS480 |
| C | LEU523 |
| C | ASN525 |
| C | HOH640 |
| C | HOH657 |
| C | HOH689 |
| C | HOH735 |
| C | HOH762 |
| C | HOH766 |
| C | HOH768 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD D 608 |
| Chain | Residue |
| D | GLY479 |
| D | HIS480 |
| D | LEU523 |
| D | ASN525 |
| D | HOH612 |
| D | HOH686 |
| D | HOH705 |
| D | HOH708 |
| D | HOH739 |
| D | HOH740 |
| B | LYS605 |
| D | ASP369 |
| D | ASN370 |
| D | GLY399 |
| D | GLY401 |
| D | GLU402 |
| D | VAL403 |
| D | THR421 |
| D | GLU422 |
| D | ILE423 |
| D | ASP424 |
| D | CYS427 |
| D | CYS454 |
| D | THR455 |
| D | GLY456 |
| D | ASN457 |
| D | MET478 |
Functional Information from PROSITE/UniProt
| site_id | PS00738 |
| Number of Residues | 15 |
| Details | ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. ACNiYSTLNeVAAAL |
| Chain | Residue | Details |
| A | ALA257-LEU271 | |
| site_id | PS00739 |
| Number of Residues | 18 |
| Details | ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKqvvVcGYGeVGKGccA |
| Chain | Residue | Details |
| A | GLY392-ALA409 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | THR236 | |
| B | GLU335 | |
| B | SER336 | |
| B | LYS365 | |
| B | ASP369 | |
| B | ASN370 | |
| C | THR236 | |
| C | ASP310 | |
| C | GLU335 | |
| C | SER336 | |
| C | LYS365 | |
| A | ASP310 | |
| C | ASP369 | |
| C | ASN370 | |
| D | THR236 | |
| D | ASP310 | |
| D | GLU335 | |
| D | SER336 | |
| D | LYS365 | |
| D | ASP369 | |
| D | ASN370 | |
| A | GLU335 | |
| A | SER336 | |
| A | LYS365 | |
| A | ASP369 | |
| A | ASN370 | |
| B | THR236 | |
| B | ASP310 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|Ref.12 |
| Chain | Residue | Details |
| A | GLY401 | |
| B | ASN525 | |
| C | GLY401 | |
| C | GLU422 | |
| C | ASN457 | |
| C | MET478 | |
| C | ASN525 | |
| D | GLY401 | |
| D | GLU422 | |
| D | ASN457 | |
| D | MET478 | |
| A | GLU422 | |
| D | ASN525 | |
| A | ASN457 | |
| A | MET478 | |
| A | ASN525 | |
| B | GLY401 | |
| B | GLU422 | |
| B | ASN457 | |
| B | MET478 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| A | HIS480 | |
| A | ASP310 | |
| A | CYS374 | |
| A | HIS234 | |
| A | ASN370 | |
| A | ASP369 | |
| A | LYS365 | |
| site_id | CSA2 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| B | HIS480 | |
| B | ASP310 | |
| B | CYS374 | |
| B | HIS234 | |
| B | ASN370 | |
| B | ASP369 | |
| B | LYS365 | |
| site_id | CSA3 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| C | HIS480 | |
| C | ASP310 | |
| C | CYS374 | |
| C | HIS234 | |
| C | ASN370 | |
| C | ASP369 | |
| C | LYS365 | |
| site_id | CSA4 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1b3r |
| Chain | Residue | Details |
| D | HIS480 | |
| D | ASP310 | |
| D | CYS374 | |
| D | HIS234 | |
| D | ASN370 | |
| D | ASP369 | |
| D | LYS365 | |
