6F3N
Crystal structure of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa cocrystallized with SAH in the presence of K+ and Zn2+ cations
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 |
| 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 |
| C | 0071269 | biological_process | L-homocysteine biosynthetic process |
| 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 |
| D | 0071269 | biological_process | L-homocysteine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue K A 501 |
| Chain | Residue |
| A | GLN65 |
| A | THR380 |
| A | HIS382 |
| A | HOH820 |
| A | HOH859 |
| C | HOH799 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 502 |
| Chain | Residue |
| A | HIS323 |
| A | ADN505 |
| A | HIS61 |
| A | CYS85 |
| A | ASP139 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 503 |
| Chain | Residue |
| A | ARG25 |
| A | ILE29 |
| A | GLU32 |
| A | HOH648 |
| C | HIS360 |
| site_id | AC4 |
| Number of Residues | 32 |
| Details | binding site for residue NAD A 504 |
| Chain | Residue |
| A | THR165 |
| A | THR166 |
| A | THR167 |
| A | ASN199 |
| A | ILE227 |
| A | GLY228 |
| A | GLY230 |
| A | ASP231 |
| A | VAL232 |
| A | GLU251 |
| A | VAL252 |
| A | ASP253 |
| A | CYS256 |
| A | THR297 |
| A | THR298 |
| A | GLY299 |
| A | ASN300 |
| A | VAL303 |
| A | ILE321 |
| A | GLY322 |
| A | HIS323 |
| A | ASN375 |
| A | HIS382 |
| A | ADN505 |
| A | HOH614 |
| A | HOH780 |
| A | HOH790 |
| A | HOH804 |
| A | HOH846 |
| A | HOH850 |
| B | LYS463 |
| B | TYR467 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | binding site for residue ADN A 505 |
| Chain | Residue |
| A | HIS61 |
| A | THR63 |
| A | GLN65 |
| A | THR66 |
| A | ASP139 |
| A | GLU164 |
| A | THR165 |
| A | LYS194 |
| A | ASP198 |
| A | HIS323 |
| A | LEU373 |
| A | THR380 |
| A | HIS382 |
| A | MET387 |
| A | PHE391 |
| A | ZN502 |
| A | NAD504 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue K B 501 |
| Chain | Residue |
| B | GLN65 |
| B | THR380 |
| B | HIS382 |
| B | HOH777 |
| B | HOH802 |
| D | HOH785 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 502 |
| Chain | Residue |
| B | HIS61 |
| B | CYS85 |
| B | ASP139 |
| B | HIS323 |
| B | ADN505 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 B 503 |
| Chain | Residue |
| B | ARG25 |
| B | ILE29 |
| B | GLU32 |
| B | HOH716 |
| B | HOH790 |
| D | HIS360 |
| site_id | AC9 |
| Number of Residues | 33 |
| Details | binding site for residue NAD B 504 |
| Chain | Residue |
| B | GLY299 |
| B | ASN300 |
| B | VAL303 |
| B | ILE321 |
| B | GLY322 |
| B | HIS323 |
| B | LEU373 |
| B | ASN375 |
| B | HIS382 |
| B | ADN505 |
| B | HOH708 |
| B | HOH753 |
| B | HOH801 |
| B | HOH821 |
| B | HOH827 |
| B | HOH875 |
| A | LYS463 |
| A | TYR467 |
| B | THR165 |
| B | THR166 |
| B | THR167 |
| B | ASN199 |
| B | ILE227 |
| B | GLY228 |
| B | GLY230 |
| B | ASP231 |
| B | VAL232 |
| B | GLU251 |
| B | VAL252 |
| B | ASP253 |
| B | CYS256 |
| B | THR297 |
| B | THR298 |
| site_id | AD1 |
| Number of Residues | 16 |
| Details | binding site for residue ADN B 505 |
| Chain | Residue |
| B | HIS61 |
| B | THR63 |
| B | GLN65 |
| B | THR66 |
| B | ASP139 |
| B | GLU164 |
| B | THR165 |
| B | LYS194 |
| B | ASP198 |
| B | HIS323 |
| B | LEU373 |
| B | THR380 |
| B | HIS382 |
| B | MET387 |
| B | ZN502 |
| B | NAD504 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue K C 501 |
| Chain | Residue |
| C | GLN65 |
| C | THR380 |
| C | HIS382 |
| C | HOH734 |
| C | HOH784 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue ZN C 502 |
| Chain | Residue |
| C | HIS61 |
| C | CYS85 |
| C | ASP139 |
| C | HIS323 |
| C | ADN505 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 C 503 |
| Chain | Residue |
| A | HIS360 |
| C | ARG25 |
| C | ILE29 |
| C | GLU32 |
| C | HOH673 |
| site_id | AD5 |
| Number of Residues | 32 |
| Details | binding site for residue NAD C 504 |
| Chain | Residue |
| C | THR165 |
| C | THR166 |
| C | THR167 |
| C | ASN199 |
| C | ILE227 |
| C | GLY228 |
| C | GLY230 |
| C | ASP231 |
| C | VAL232 |
| C | GLU251 |
| C | VAL252 |
| C | ASP253 |
| C | CYS256 |
| C | THR297 |
| C | THR298 |
| C | GLY299 |
| C | ASN300 |
| C | VAL303 |
| C | ILE321 |
| C | GLY322 |
| C | HIS323 |
| C | LEU373 |
| C | ASN375 |
| C | HIS382 |
| C | ADN505 |
| C | HOH723 |
| C | HOH754 |
| C | HOH773 |
| C | HOH787 |
| C | HOH792 |
| D | LYS463 |
| D | TYR467 |
| site_id | AD6 |
| Number of Residues | 17 |
| Details | binding site for residue ADN C 505 |
| Chain | Residue |
| C | HIS61 |
| C | THR63 |
| C | GLN65 |
| C | THR66 |
| C | ASP139 |
| C | GLU164 |
| C | THR165 |
| C | LYS194 |
| C | ASP198 |
| C | HIS323 |
| C | LEU373 |
| C | THR380 |
| C | HIS382 |
| C | MET387 |
| C | PHE391 |
| C | ZN502 |
| C | NAD504 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue K D 501 |
| Chain | Residue |
| B | HOH847 |
| D | GLN65 |
| D | THR380 |
| D | HIS382 |
| D | HOH752 |
| D | HOH835 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue ZN D 502 |
| Chain | Residue |
| D | HIS61 |
| D | CYS85 |
| D | ASP139 |
| D | HIS323 |
| D | ADN506 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 D 503 |
| Chain | Residue |
| B | HIS360 |
| D | ARG25 |
| D | ILE29 |
| D | GLU32 |
| D | HOH617 |
| D | HOH828 |
| site_id | AE1 |
| Number of Residues | 7 |
| Details | binding site for residue GOL D 504 |
| Chain | Residue |
| B | GLU121 |
| B | GLN122 |
| B | GLY128 |
| D | THR11 |
| D | TYR13 |
| D | HOH760 |
| D | HOH893 |
| site_id | AE2 |
| Number of Residues | 31 |
| Details | binding site for residue NAD D 505 |
| Chain | Residue |
| C | LYS463 |
| C | TYR467 |
| D | THR165 |
| D | THR166 |
| D | THR167 |
| D | ASN199 |
| D | ILE227 |
| D | GLY228 |
| D | GLY230 |
| D | ASP231 |
| D | VAL232 |
| D | GLU251 |
| D | VAL252 |
| D | ASP253 |
| D | CYS256 |
| D | THR297 |
| D | THR298 |
| D | GLY299 |
| D | ASN300 |
| D | VAL303 |
| D | ILE321 |
| D | GLY322 |
| D | HIS323 |
| D | ASN375 |
| D | HIS382 |
| D | ADN506 |
| D | HOH757 |
| D | HOH758 |
| D | HOH790 |
| D | HOH795 |
| D | HOH861 |
| site_id | AE3 |
| Number of Residues | 16 |
| Details | binding site for residue ADN D 506 |
| Chain | Residue |
| D | HIS61 |
| D | THR63 |
| D | GLN65 |
| D | THR66 |
| D | ASP139 |
| D | GLU164 |
| D | THR165 |
| D | LYS194 |
| D | ASP198 |
| D | HIS323 |
| D | LEU373 |
| D | THR380 |
| D | HIS382 |
| D | MET387 |
| D | ZN502 |
| D | NAD505 |
Functional Information from PROSITE/UniProt
| site_id | PS00738 |
| Number of Residues | 15 |
| Details | ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiFSTQDqAAAAI |
| Chain | Residue | Details |
| A | SER84-ILE98 |
| site_id | PS00739 |
| Number of Residues | 17 |
| Details | ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKqalViGYGdVGKGs.S |
| Chain | Residue | Details |
| A | GLY221-SER237 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 72 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00563","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
