3N58
Crystal structure of S-ADENOSYL-L-HOMOCYSTEINE hydrolase from brucella melitensis in ternary complex with NAD and adenosine, orthorhombic form
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 |
| 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 | 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 | 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 | 5 |
| Details | BINDING SITE FOR RESIDUE K A 2 |
| Chain | Residue |
| A | GLN59 |
| A | THR385 |
| A | GLY386 |
| A | HIS387 |
| A | HOH521 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADN A 500 |
| Chain | Residue |
| A | ASP132 |
| A | GLU192 |
| A | THR193 |
| A | LYS222 |
| A | ASP226 |
| A | HIS337 |
| A | LEU378 |
| A | THR385 |
| A | HIS387 |
| A | MET392 |
| A | NAD550 |
| A | HIS55 |
| A | THR57 |
| A | GLN59 |
| A | THR60 |
| site_id | AC3 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD A 550 |
| Chain | Residue |
| A | THR193 |
| A | THR194 |
| A | THR195 |
| A | ASP226 |
| A | ASN227 |
| A | GLY256 |
| A | GLY258 |
| A | ASP259 |
| A | VAL260 |
| A | THR278 |
| A | GLU279 |
| A | VAL280 |
| A | ASP281 |
| A | CYS284 |
| A | THR311 |
| A | THR312 |
| A | GLY313 |
| A | ASN314 |
| A | ILE335 |
| A | GLY336 |
| A | HIS337 |
| A | ASN380 |
| A | HIS387 |
| A | HOH471 |
| A | HOH479 |
| A | HOH492 |
| A | ADN500 |
| A | HOH534 |
| A | HOH577 |
| A | HOH653 |
| B | LYS460 |
| B | TYR464 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD B 550 |
| Chain | Residue |
| A | LYS460 |
| A | TYR464 |
| B | ASN227 |
| B | GLY256 |
| B | GLY258 |
| B | ASP259 |
| B | VAL260 |
| B | THR278 |
| B | GLU279 |
| B | VAL280 |
| B | ASP281 |
| B | CYS284 |
| B | THR311 |
| B | THR312 |
| B | GLY313 |
| B | ASN314 |
| B | ILE335 |
| B | GLY336 |
| B | HIS337 |
| B | ASN380 |
| B | HIS387 |
| B | HOH498 |
| B | HOH523 |
| B | HOH526 |
| B | HOH543 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C 1 |
| Chain | Residue |
| C | GLN59 |
| C | THR385 |
| C | GLY386 |
| C | HIS387 |
| C | HOH479 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ADN C 500 |
| Chain | Residue |
| C | NAD550 |
| C | LEU54 |
| C | HIS55 |
| C | THR57 |
| C | GLN59 |
| C | THR60 |
| C | ASP132 |
| C | GLU192 |
| C | THR193 |
| C | LYS222 |
| C | ASP226 |
| C | HIS337 |
| C | LEU378 |
| C | THR385 |
| C | GLY386 |
| C | HIS387 |
| C | MET392 |
| C | PHE396 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD C 550 |
| Chain | Residue |
| C | THR193 |
| C | THR194 |
| C | THR195 |
| C | ASN227 |
| C | GLY256 |
| C | GLY258 |
| C | ASP259 |
| C | VAL260 |
| C | THR278 |
| C | GLU279 |
| C | VAL280 |
| C | ASP281 |
| C | THR311 |
| C | THR312 |
| C | GLY313 |
| C | ASN314 |
| C | ILE335 |
| C | GLY336 |
| C | HIS337 |
| C | ASN380 |
| C | HIS387 |
| C | HOH473 |
| C | HOH478 |
| C | ADN500 |
| C | HOH512 |
| C | HOH539 |
| C | HOH578 |
| C | HOH579 |
| D | LYS460 |
| D | TYR464 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K D 467 |
| Chain | Residue |
| D | GLN59 |
| D | THR385 |
| D | GLY386 |
| D | HIS387 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADN D 500 |
| Chain | Residue |
| D | LEU54 |
| D | HIS55 |
| D | THR57 |
| D | GLN59 |
| D | THR60 |
| D | ASP132 |
| D | GLU192 |
| D | THR193 |
| D | LYS222 |
| D | ASP226 |
| D | HIS337 |
| D | LEU378 |
| D | THR385 |
| D | HIS387 |
| D | MET392 |
| D | PHE396 |
| D | NAD550 |
| site_id | BC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD D 550 |
| Chain | Residue |
| C | GLN447 |
| C | LYS460 |
| C | TYR464 |
| C | HOH490 |
| D | THR193 |
| D | THR194 |
| D | THR195 |
| D | ASN227 |
| D | GLY256 |
| D | GLY258 |
| D | ASP259 |
| D | VAL260 |
| D | THR278 |
| D | GLU279 |
| D | VAL280 |
| D | ASP281 |
| D | CYS284 |
| D | THR311 |
| D | THR312 |
| D | GLY313 |
| D | ASN314 |
| D | ILE335 |
| D | GLY336 |
| D | HIS337 |
| D | LEU378 |
| D | ASN380 |
| D | HIS387 |
| D | HOH482 |
| D | ADN500 |
| D | HOH511 |
| D | HOH516 |
Functional Information from PROSITE/UniProt
| site_id | PS00738 |
| Number of Residues | 15 |
| Details | ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiFSTQDhAAAAI |
| Chain | Residue | Details |
| A | SER78-ILE92 |
| site_id | PS00739 |
| Number of Residues | 17 |
| Details | ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKvavVcGYGdVGKGs.A |
| Chain | Residue | Details |
| A | GLY249-ALA265 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00563 |
| Chain | Residue | Details |
| A | THR57 | |
| A | ASN314 | |
| A | ILE335 | |
| A | ASN380 | |
| B | THR57 | |
| B | ASP132 | |
| B | GLU192 | |
| B | THR193 | |
| B | LYS222 | |
| B | ASP226 | |
| B | ASN227 | |
| A | ASP132 | |
| B | GLY256 | |
| B | GLU279 | |
| B | ASN314 | |
| B | ILE335 | |
| B | ASN380 | |
| C | THR57 | |
| C | ASP132 | |
| C | GLU192 | |
| C | THR193 | |
| C | LYS222 | |
| A | GLU192 | |
| C | ASP226 | |
| C | ASN227 | |
| C | GLY256 | |
| C | GLU279 | |
| C | ASN314 | |
| C | ILE335 | |
| C | ASN380 | |
| D | THR57 | |
| D | ASP132 | |
| D | GLU192 | |
| A | THR193 | |
| D | THR193 | |
| D | LYS222 | |
| D | ASP226 | |
| D | ASN227 | |
| D | GLY256 | |
| D | GLU279 | |
| D | ASN314 | |
| D | ILE335 | |
| D | ASN380 | |
| A | LYS222 | |
| A | ASP226 | |
| A | ASN227 | |
| A | GLY256 | |
| A | GLU279 |
