5HXD
Crystal structure of murein-tripeptide amidase MpaA from Escherichia coli O157
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004040 | molecular_function | amidase activity |
| A | 0004180 | molecular_function | carboxypeptidase activity |
| A | 0004181 | molecular_function | metallocarboxypeptidase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009253 | biological_process | peptidoglycan catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016998 | biological_process | cell wall macromolecule catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0061473 | molecular_function | murein tripeptide carboxypeptidase activity |
| A | 0071555 | biological_process | cell wall organization |
| B | 0004040 | molecular_function | amidase activity |
| B | 0004180 | molecular_function | carboxypeptidase activity |
| B | 0004181 | molecular_function | metallocarboxypeptidase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009253 | biological_process | peptidoglycan catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016998 | biological_process | cell wall macromolecule catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0061473 | molecular_function | murein tripeptide carboxypeptidase activity |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | HIS49 |
| A | GLU52 |
| A | HIS157 |
| A | ASP158 |
| A | CAC302 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue CAC A 302 |
| Chain | Residue |
| A | VAL187 |
| A | TYR189 |
| A | GLU210 |
| A | ZN301 |
| A | HIS49 |
| A | ASN98 |
| A | ARG99 |
| A | HIS157 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | HIS49 |
| B | GLU52 |
| B | HIS157 |
| B | ASP158 |
| B | CAC302 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue CAC B 302 |
| Chain | Residue |
| B | HIS49 |
| B | ARG89 |
| B | ASN98 |
| B | ARG99 |
| B | ZN301 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 233 |
| Details | Domain: {"description":"Peptidase M14","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
