3BPB
Crystal structure of the dimethylarginine dimethylaminohydrolase H162G adduct with S-methyl-L-thiocitrulline
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000052 | biological_process | citrulline metabolic process |
A | 0006525 | biological_process | arginine metabolic process |
A | 0016403 | molecular_function | dimethylargininase activity |
A | 0016597 | molecular_function | amino acid binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0045429 | biological_process | positive regulation of nitric oxide biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0000052 | biological_process | citrulline metabolic process |
B | 0006525 | biological_process | arginine metabolic process |
B | 0016403 | molecular_function | dimethylargininase activity |
B | 0016597 | molecular_function | amino acid binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0045429 | biological_process | positive regulation of nitric oxide biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SMZ A 500 |
Chain | Residue |
A | LEU18 |
A | ASP244 |
A | CYS249 |
A | ASP60 |
A | PHE63 |
A | GLU65 |
A | ASP66 |
A | ARG85 |
A | GLY116 |
A | ARG132 |
A | ILE243 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SMZ B 500 |
Chain | Residue |
B | LEU18 |
B | ASP60 |
B | PHE63 |
B | GLU65 |
B | ASP66 |
B | ARG85 |
B | GLY116 |
B | ARG132 |
B | ILE243 |
B | ASP244 |
B | CYS249 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:11473257, ECO:0000305|PubMed:16634643, ECO:0000305|PubMed:18482699 |
Chain | Residue | Details |
A | GLY162 | |
B | GLY162 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:11473257, ECO:0000305|PubMed:16634643, ECO:0000305|PubMed:18482699 |
Chain | Residue | Details |
A | CYS249 | |
B | CYS249 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000305|PubMed:11473257 |
Chain | Residue | Details |
A | LEU18 | |
B | ARG85 | |
B | ARG132 | |
B | ILE243 | |
A | ASP60 | |
A | GLU65 | |
A | ARG85 | |
A | ARG132 | |
A | ILE243 | |
B | LEU18 | |
B | ASP60 | |
B | GLU65 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:16634643 |
Chain | Residue | Details |
A | GLY162 | |
A | CYS249 | |
B | GLY162 | |
B | CYS249 |