6F3M
Crystal structure of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa complexed with adenosine, 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 | 33 |
Details | binding site for residue NAD A 501 |
Chain | Residue |
A | THR165 |
A | GLU251 |
A | VAL252 |
A | ASP253 |
A | CYS256 |
A | THR297 |
A | THR298 |
A | GLY299 |
A | ASN300 |
A | VAL303 |
A | ILE321 |
A | THR166 |
A | GLY322 |
A | HIS323 |
A | LEU373 |
A | ASN375 |
A | HIS382 |
A | ADN502 |
A | HOH692 |
A | HOH717 |
A | HOH725 |
A | HOH783 |
A | THR167 |
A | HOH831 |
A | HOH851 |
B | LYS463 |
B | TYR467 |
A | ASN199 |
A | ILE227 |
A | GLY228 |
A | GLY230 |
A | ASP231 |
A | VAL232 |
site_id | AC2 |
Number of Residues | 17 |
Details | binding site for residue ADN A 502 |
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 | NAD501 |
A | ZN506 |
site_id | AC3 |
Number of Residues | 10 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | ASP465 |
A | THR466 |
A | TYR467 |
A | ARG468 |
A | HOH646 |
A | HOH879 |
B | ASP465 |
B | THR466 |
B | TYR467 |
B | ARG468 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue PO4 A 504 |
Chain | Residue |
A | ARG25 |
A | GLU32 |
A | HOH714 |
A | HOH816 |
A | HOH894 |
C | HIS360 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue K A 505 |
Chain | Residue |
A | GLN65 |
A | THR380 |
A | HIS382 |
A | HOH794 |
A | HOH824 |
C | HOH771 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue ZN A 506 |
Chain | Residue |
A | HIS61 |
A | CYS85 |
A | ASP139 |
A | HIS323 |
A | ADN502 |
site_id | AC7 |
Number of Residues | 33 |
Details | binding site for residue NAD B 501 |
Chain | Residue |
B | HIS323 |
B | LEU373 |
B | ASN375 |
B | HIS382 |
B | ADN502 |
B | HOH723 |
B | HOH782 |
B | HOH829 |
B | HOH855 |
B | HOH858 |
B | HOH895 |
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 |
B | GLY299 |
B | ASN300 |
B | VAL303 |
B | ILE321 |
B | GLY322 |
site_id | AC8 |
Number of Residues | 17 |
Details | binding site for residue ADN B 502 |
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 | PHE391 |
B | NAD501 |
B | ZN505 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue PO4 B 503 |
Chain | Residue |
B | ARG25 |
B | ILE29 |
B | GLU32 |
B | HOH681 |
B | HOH711 |
D | HIS360 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue K B 504 |
Chain | Residue |
B | GLN65 |
B | THR380 |
B | HIS382 |
B | HOH769 |
B | HOH797 |
D | HOH819 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue ZN B 505 |
Chain | Residue |
B | HIS61 |
B | CYS85 |
B | ASP139 |
B | HIS323 |
B | ADN502 |
site_id | AD3 |
Number of Residues | 33 |
Details | binding site for residue NAD C 501 |
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 | ADN502 |
C | HOH697 |
C | HOH760 |
C | HOH786 |
C | HOH850 |
C | HOH866 |
C | HOH924 |
D | LYS463 |
D | TYR467 |
site_id | AD4 |
Number of Residues | 17 |
Details | binding site for residue ADN C 502 |
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 | NAD501 |
C | ZN506 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for residue GOL C 503 |
Chain | Residue |
C | THR167 |
C | HIS170 |
C | GLY299 |
C | HOH680 |
C | HOH880 |
D | TYR453 |
D | HOH663 |
D | HOH710 |
site_id | AD6 |
Number of Residues | 7 |
Details | binding site for residue PO4 C 504 |
Chain | Residue |
A | HIS360 |
C | ARG25 |
C | ILE29 |
C | GLU32 |
C | HOH645 |
C | HOH686 |
C | HOH955 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue K C 505 |
Chain | Residue |
A | HOH751 |
C | GLN65 |
C | THR380 |
C | HIS382 |
C | HOH819 |
C | HOH851 |
site_id | AD8 |
Number of Residues | 5 |
Details | binding site for residue ZN C 506 |
Chain | Residue |
C | HIS61 |
C | CYS85 |
C | ASP139 |
C | HIS323 |
C | ADN502 |
site_id | AD9 |
Number of Residues | 33 |
Details | binding site for residue NAD D 501 |
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 | LEU373 |
D | ASN375 |
D | HIS382 |
D | ADN502 |
D | HOH701 |
D | HOH727 |
D | HOH850 |
D | HOH852 |
D | HOH868 |
D | HOH931 |
site_id | AE1 |
Number of Residues | 17 |
Details | binding site for residue ADN D 502 |
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 | PHE391 |
D | NAD501 |
D | ZN506 |
site_id | AE2 |
Number of Residues | 7 |
Details | binding site for residue GOL D 503 |
Chain | Residue |
C | TYR453 |
D | THR167 |
D | HIS170 |
D | GLY299 |
D | HOH629 |
D | HOH664 |
D | HOH887 |
site_id | AE3 |
Number of Residues | 6 |
Details | binding site for residue PO4 D 504 |
Chain | Residue |
B | HIS360 |
D | ARG25 |
D | ILE29 |
D | GLU32 |
D | HOH642 |
D | HOH763 |
site_id | AE4 |
Number of Residues | 5 |
Details | binding site for residue K D 505 |
Chain | Residue |
D | GLN65 |
D | THR380 |
D | HIS382 |
D | HOH836 |
D | HOH872 |
site_id | AE5 |
Number of Residues | 5 |
Details | binding site for residue ZN D 506 |
Chain | Residue |
D | HIS61 |
D | CYS85 |
D | ASP139 |
D | HIS323 |
D | ADN502 |
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 |
B | SER84-ILE98 | |
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 |
B | GLY221-SER237 | |
A | GLY221-SER237 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 36 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00563 |
Chain | Residue | Details |
B | THR63 | |
B | ASN300 | |
B | ILE321 | |
B | ASN375 | |
C | THR63 | |
C | ASP139 | |
C | GLU164 | |
C | THR165 | |
C | LYS194 | |
C | ASP198 | |
C | ASN199 | |
B | ASP139 | |
C | GLY228 | |
C | GLU251 | |
C | ASN300 | |
C | ILE321 | |
C | ASN375 | |
D | THR63 | |
D | ASP139 | |
D | GLU164 | |
D | THR165 | |
D | LYS194 | |
B | GLU164 | |
D | ASP198 | |
D | ASN199 | |
D | GLY228 | |
D | GLU251 | |
D | ASN300 | |
D | ILE321 | |
D | ASN375 | |
B | THR165 | |
B | LYS194 | |
B | ASP198 | |
B | ASN199 | |
B | GLY228 | |
B | GLU251 |