2Y2D
crystal structure of AmpD holoenzyme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008745 | molecular_function | N-acetylmuramoyl-L-alanine amidase activity |
| A | 0009253 | biological_process | peptidoglycan catabolic process |
| A | 0009254 | biological_process | peptidoglycan turnover |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071555 | biological_process | cell wall organization |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008745 | molecular_function | N-acetylmuramoyl-L-alanine amidase activity |
| B | 0009253 | biological_process | peptidoglycan catabolic process |
| B | 0009254 | biological_process | peptidoglycan turnover |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071555 | biological_process | cell wall organization |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008745 | molecular_function | N-acetylmuramoyl-L-alanine amidase activity |
| C | 0009253 | biological_process | peptidoglycan catabolic process |
| C | 0009254 | biological_process | peptidoglycan turnover |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1180 |
| Chain | Residue |
| A | HIS34 |
| A | HIS154 |
| A | ASP164 |
| A | HOH2273 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1180 |
| Chain | Residue |
| B | HIS34 |
| B | HIS154 |
| B | ASP164 |
| B | HOH2314 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 1180 |
| Chain | Residue |
| C | HIS154 |
| C | ASP164 |
| C | HOH2276 |
| C | HIS34 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 411 |
| Details | Domain: {"description":"N-acetylmuramoyl-L-alanine amidase","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P75820","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12654266","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P75820","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
