7CJ9
Crystal structure of N-terminal His-tagged D-allulose 3-epimerase from Methylomonas sp. with additional C-terminal residues
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0016853 | molecular_function | isomerase activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0016853 | molecular_function | isomerase activity |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0016853 | molecular_function | isomerase activity |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0016853 | molecular_function | isomerase activity |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 301 |
| Chain | Residue |
| A | GLU152 |
| A | ASP185 |
| A | HIS211 |
| A | GLU246 |
| A | FUD302 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue FUD A 302 |
| Chain | Residue |
| A | GLY110 |
| A | VAL111 |
| A | GLU152 |
| A | GLU158 |
| A | ASP185 |
| A | HIS188 |
| A | HIS211 |
| A | ARG217 |
| A | GLU246 |
| A | LEU261 |
| A | MN301 |
| A | HIS12 |
| A | SER69 |
| A | LEU70 |
| A | GLY71 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue EPE A 303 |
| Chain | Residue |
| A | ARG128 |
| A | ASN160 |
| A | ILE161 |
| A | ASN163 |
| A | GLU167 |
| A | HOH541 |
| B | TRP264 |
| B | ARG265 |
| C | LYS27 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MN B 301 |
| Chain | Residue |
| B | GLU152 |
| B | ASP185 |
| B | HIS211 |
| B | GLU246 |
| B | FUD302 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residue FUD B 302 |
| Chain | Residue |
| B | HIS12 |
| B | SER69 |
| B | LEU70 |
| B | VAL111 |
| B | GLU152 |
| B | GLU158 |
| B | ASP185 |
| B | HIS188 |
| B | HIS211 |
| B | ARG217 |
| B | GLU246 |
| B | LEU261 |
| B | MN301 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue EPE B 303 |
| Chain | Residue |
| A | TRP264 |
| A | ARG265 |
| B | ARG125 |
| B | ASN160 |
| B | ILE161 |
| B | ASN163 |
| B | GLU167 |
| B | HOH409 |
| D | LYS27 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 301 |
| Chain | Residue |
| C | ALA197 |
| C | SER229 |
| C | ALA232 |
| C | ALA233 |
| C | GLN236 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO C 302 |
| Chain | Residue |
| C | ALA115 |
| C | GLY117 |
| C | LYS118 |
| C | TYR119 |
| C | HOH408 |
| C | HOH454 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 303 |
| Chain | Residue |
| C | LEU7 |
| C | ASP38 |
| C | LYS283 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MN C 304 |
| Chain | Residue |
| C | GLU152 |
| C | ASP185 |
| C | HIS211 |
| C | GLU246 |
| C | FUD305 |
| site_id | AD2 |
| Number of Residues | 12 |
| Details | binding site for residue FUD C 305 |
| Chain | Residue |
| C | HIS12 |
| C | SER69 |
| C | VAL111 |
| C | GLU152 |
| C | GLU158 |
| C | ASP185 |
| C | HIS188 |
| C | HIS211 |
| C | ARG217 |
| C | GLU246 |
| C | LEU261 |
| C | MN304 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue EPE C 306 |
| Chain | Residue |
| A | LYS27 |
| C | ARG128 |
| C | ASN160 |
| C | ILE161 |
| C | ASN163 |
| C | GLU167 |
| D | TRP264 |
| D | ARG265 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 301 |
| Chain | Residue |
| D | GLY117 |
| D | LYS118 |
| D | TYR119 |
| D | HOH462 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue MN D 302 |
| Chain | Residue |
| D | GLU152 |
| D | ASP185 |
| D | HIS211 |
| D | GLU246 |
| D | FUD303 |
| site_id | AD6 |
| Number of Residues | 13 |
| Details | binding site for residue FUD D 303 |
| Chain | Residue |
| D | HIS12 |
| D | GLU41 |
| D | SER69 |
| D | VAL111 |
| D | GLU152 |
| D | GLU158 |
| D | ASP185 |
| D | HIS188 |
| D | HIS211 |
| D | ARG217 |
| D | GLU246 |
| D | LEU261 |
| D | MN302 |
| site_id | AD7 |
| Number of Residues | 10 |
| Details | binding site for residue EPE D 304 |
| Chain | Residue |
| B | LYS27 |
| C | TRP264 |
| C | ARG265 |
| D | ARG128 |
| D | ASN160 |
| D | ILE161 |
| D | ASN163 |
| D | GLU167 |
| D | HOH497 |
| D | HOH551 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO E 301 |
| Chain | Residue |
| E | ALA115 |
| E | GLY117 |
| E | LYS118 |
| E | HOH476 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue MN E 302 |
| Chain | Residue |
| E | GLU152 |
| E | ASP185 |
| E | HIS211 |
| E | GLU246 |
| E | FUD303 |
| site_id | AE1 |
| Number of Residues | 14 |
| Details | binding site for residue FUD E 303 |
| Chain | Residue |
| E | HIS12 |
| E | SER69 |
| E | LEU70 |
| E | GLY110 |
| E | VAL111 |
| E | GLU152 |
| E | GLU158 |
| E | ASP185 |
| E | HIS188 |
| E | HIS211 |
| E | ARG217 |
| E | GLU246 |
| E | LEU261 |
| E | MN302 |
| site_id | AE2 |
| Number of Residues | 10 |
| Details | binding site for residue EPE E 304 |
| Chain | Residue |
| E | ARG128 |
| E | ASN160 |
| E | ILE161 |
| E | ASN163 |
| E | GLU167 |
| E | HOH449 |
| E | HOH548 |
| F | TRP264 |
| F | ARG265 |
| G | LYS27 |
| site_id | AE3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO F 301 |
| Chain | Residue |
| F | LEU45 |
| F | THR76 |
| F | LEU92 |
| F | HOH414 |
| F | HOH541 |
| site_id | AE4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO F 302 |
| Chain | Residue |
| F | ALA74 |
| F | GLY117 |
| F | LYS118 |
| F | TYR119 |
| F | HOH406 |
| F | HOH415 |
| F | HOH495 |
| site_id | AE5 |
| Number of Residues | 5 |
| Details | binding site for residue MN F 303 |
| Chain | Residue |
| F | GLU152 |
| F | ASP185 |
| F | HIS211 |
| F | GLU246 |
| F | FUD304 |
| site_id | AE6 |
| Number of Residues | 13 |
| Details | binding site for residue FUD F 304 |
| Chain | Residue |
| F | HIS12 |
| F | LEU45 |
| F | SER69 |
| F | VAL111 |
| F | GLU152 |
| F | GLU158 |
| F | ASP185 |
| F | HIS188 |
| F | HIS211 |
| F | ARG217 |
| F | GLU246 |
| F | LEU261 |
| F | MN303 |
| site_id | AE7 |
| Number of Residues | 10 |
| Details | binding site for residue EPE F 305 |
| Chain | Residue |
| E | TRP264 |
| E | ARG265 |
| F | ARG125 |
| F | ARG128 |
| F | ASN160 |
| F | ILE161 |
| F | ASN163 |
| F | GLU167 |
| F | HOH434 |
| H | LYS27 |
| site_id | AE8 |
| Number of Residues | 5 |
| Details | binding site for residue MN G 301 |
| Chain | Residue |
| G | GLU152 |
| G | ASP185 |
| G | HIS211 |
| G | GLU246 |
| G | FUD302 |
| site_id | AE9 |
| Number of Residues | 15 |
| Details | binding site for residue FUD G 302 |
| Chain | Residue |
| G | HIS12 |
| G | ALA43 |
| G | SER69 |
| G | LEU70 |
| G | GLY110 |
| G | VAL111 |
| G | GLU152 |
| G | GLU158 |
| G | ASP185 |
| G | HIS188 |
| G | HIS211 |
| G | ARG217 |
| G | GLU246 |
| G | LEU261 |
| G | MN301 |
| site_id | AF1 |
| Number of Residues | 8 |
| Details | binding site for residue EPE G 303 |
| Chain | Residue |
| E | LYS27 |
| G | ASN160 |
| G | ILE161 |
| G | ASN163 |
| G | GLU167 |
| G | HOH414 |
| H | TRP264 |
| H | ARG265 |
| site_id | AF2 |
| Number of Residues | 5 |
| Details | binding site for residue MN H 301 |
| Chain | Residue |
| H | GLU152 |
| H | ASP185 |
| H | HIS211 |
| H | GLU246 |
| H | FUD302 |
| site_id | AF3 |
| Number of Residues | 15 |
| Details | binding site for residue FUD H 302 |
| Chain | Residue |
| H | HIS12 |
| H | SER69 |
| H | LEU70 |
| H | GLY71 |
| H | GLY110 |
| H | VAL111 |
| H | GLU152 |
| H | GLU158 |
| H | ASP185 |
| H | HIS188 |
| H | HIS211 |
| H | ARG217 |
| H | GLU246 |
| H | LEU261 |
| H | MN301 |
| site_id | AF4 |
| Number of Residues | 10 |
| Details | binding site for residue EPE H 303 |
| Chain | Residue |
| F | LYS27 |
| G | TRP264 |
| G | ARG265 |
| H | ARG128 |
| H | ASN160 |
| H | ILE161 |
| H | ASN163 |
| H | GLU167 |
| H | HOH489 |
| H | HOH501 |
Functional Information from PROSITE/UniProt
| site_id | PS00105 |
| Number of Residues | 14 |
| Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. GMAKsvLAaGDRLG |
| Chain | Residue | Details |
| A | GLY195-GLY208 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q9WYP7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33838083","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CJ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CJ9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33838083","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CJ5","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"7CJ4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CJ6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CJ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CJ8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7CJ9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






