2Y2B
crystal structure of AmpD in complex with reaction products
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 | 13 |
Details | BINDING SITE FOR RESIDUE AH0 A 1000 |
Chain | Residue |
A | HIS34 |
A | LYS162 |
A | ASP164 |
A | MHI202 |
A | ZN203 |
A | ASN35 |
A | ILE36 |
A | LEU38 |
A | LEU51 |
A | TYR63 |
A | ILE67 |
A | GLU116 |
A | HIS154 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE MHI A 1001 |
Chain | Residue |
A | HIS34 |
A | PHE52 |
A | ARG71 |
A | VAL72 |
A | SER73 |
A | TRP95 |
A | HIS96 |
A | ALA97 |
A | GLY98 |
A | ARG107 |
A | ASN109 |
A | GLU116 |
A | HIS154 |
A | ARG161 |
A | ARG175 |
A | AH0201 |
A | ZN203 |
A | HOH414 |
A | HOH424 |
A | HOH311 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 1180 |
Chain | Residue |
A | HIS34 |
A | HIS154 |
A | ASP164 |
A | AH0201 |
A | MHI202 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 1180 |
Chain | Residue |
B | HIS34 |
B | HIS154 |
B | ASP164 |
B | HOH450 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 1180 |
Chain | Residue |
C | HIS34 |
C | HIS154 |
C | ASP164 |
C | HOH430 |
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 |