1Z9T
CRYSTAL STRUCTURE OF A PUTATIVE LACCASE (YFIH) FROM ESCHERICHIA COLI AT 1.54 A RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000270 | biological_process | peptidoglycan metabolic process |
| A | 0004000 | molecular_function | adenosine deaminase activity |
| A | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016682 | molecular_function | oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017061 | molecular_function | S-methyl-5-thioadenosine phosphorylase activity |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CIT A 244 |
| Chain | Residue |
| A | ARG115 |
| A | GLU163 |
| A | VAL164 |
| A | GLY165 |
| A | LYS189 |
| A | ARG228 |
| A | EDO248 |
| A | EDO264 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CIT A 245 |
| Chain | Residue |
| A | THR104 |
| A | ALA105 |
| A | ASP106 |
| A | CYS107 |
| A | HIS124 |
| A | TYR227 |
| A | ARG235 |
| A | HOH281 |
| A | HOH426 |
| A | HOH470 |
| A | HIS71 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 246 |
| Chain | Residue |
| A | LEU28 |
| A | ASN43 |
| A | HIS46 |
| A | VAL205 |
| A | HOH278 |
| A | HOH348 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 247 |
| Chain | Residue |
| A | ARG22 |
| A | ILE23 |
| A | GLY24 |
| A | ASP32 |
| A | SER33 |
| A | GLU222 |
| A | EDO253 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 248 |
| Chain | Residue |
| A | PRO10 |
| A | PRO12 |
| A | ARG115 |
| A | LYS189 |
| A | CIT244 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 249 |
| Chain | Residue |
| A | PRO159 |
| A | ALA181 |
| A | ALA182 |
| A | ILE184 |
| A | LEU191 |
| A | GLN196 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 250 |
| Chain | Residue |
| A | GLY58 |
| A | HOH459 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 251 |
| Chain | Residue |
| A | LEU67 |
| A | GLN69 |
| A | EDO257 |
| A | HOH412 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 252 |
| Chain | Residue |
| A | ASP106 |
| A | CYS107 |
| A | LEU108 |
| A | ALA125 |
| A | GLY126 |
| A | TRP127 |
| A | PHE162 |
| A | ILE194 |
| A | HOH407 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 253 |
| Chain | Residue |
| A | ASP32 |
| A | ASN221 |
| A | EDO247 |
| A | HOH333 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 254 |
| Chain | Residue |
| A | ASP193 |
| A | TYR195 |
| A | ARG199 |
| A | GLY213 |
| A | EDO258 |
| A | EDO263 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 255 |
| Chain | Residue |
| A | VAL139 |
| A | PHE142 |
| A | ASP144 |
| A | PRO146 |
| A | HOH289 |
| A | HOH404 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 256 |
| Chain | Residue |
| A | ARG128 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 257 |
| Chain | Residue |
| A | ARG51 |
| A | EDO251 |
| A | HOH279 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 258 |
| Chain | Residue |
| A | PRO159 |
| A | GLY213 |
| A | ARG215 |
| A | EDO254 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 259 |
| Chain | Residue |
| A | TYR218 |
| A | THR219 |
| A | ASN221 |
| A | ARG229 |
| A | HOH305 |
| A | HOH309 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 260 |
| Chain | Residue |
| A | PRO44 |
| A | ARG51 |
| A | HOH334 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 261 |
| Chain | Residue |
| A | GLU48 |
| A | LYS52 |
| A | HOH443 |
| A | HOH454 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 262 |
| Chain | Residue |
| A | PHE55 |
| A | LEU60 |
| A | SER62 |
| A | HOH445 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 263 |
| Chain | Residue |
| A | GLY212 |
| A | GLY213 |
| A | EDO254 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 264 |
| Chain | Residue |
| A | TRP127 |
| A | PHE162 |
| A | ARG228 |
| A | CIT244 |
| A | HOH389 |
| A | HOH398 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P84138","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
