2J9P
Crystal structure of the Bacillus subtilis PBP4a, and its complex with a peptidoglycan mimetic peptide.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000270 | biological_process | peptidoglycan metabolic process |
| A | 0004185 | molecular_function | serine-type carboxypeptidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006508 | biological_process | proteolysis |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0045121 | cellular_component | membrane raft |
| A | 0051301 | biological_process | cell division |
| A | 0071555 | biological_process | cell wall organization |
| B | 0000270 | biological_process | peptidoglycan metabolic process |
| B | 0004185 | molecular_function | serine-type carboxypeptidase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006508 | biological_process | proteolysis |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0045121 | cellular_component | membrane raft |
| B | 0051301 | biological_process | cell division |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE REZ A 500 |
| Chain | Residue |
| A | ALA51 |
| A | GLY413 |
| A | SER414 |
| A | LEU415 |
| A | SER416 |
| A | DAL501 |
| A | SER52 |
| A | PRO142 |
| A | ASP145 |
| A | TYR150 |
| A | ASN301 |
| A | SER348 |
| A | ILE350 |
| A | HIS352 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE REZ B 500 |
| Chain | Residue |
| B | ALA51 |
| B | SER52 |
| B | ASP145 |
| B | TYR150 |
| B | ASN301 |
| B | HIS352 |
| B | GLY413 |
| B | SER414 |
| B | LEU415 |
| B | SER416 |
| B | DAL501 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DAL B 501 |
| Chain | Residue |
| B | SER52 |
| B | SER299 |
| B | LYS411 |
| B | THR412 |
| B | GLY413 |
| B | SER414 |
| B | REZ500 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DAL A 501 |
| Chain | Residue |
| A | SER52 |
| A | SER299 |
| A | LYS411 |
| A | THR412 |
| A | GLY413 |
| A | REZ500 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Acyl-ester intermediate => ECO:0000305|PubMed:17582436 |
| Chain | Residue | Details |
| A | SER52 | |
| B | SER52 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:17582436 |
| Chain | Residue | Details |
| A | LYS55 | |
| B | LYS55 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:17582436 |
| Chain | Residue | Details |
| A | SER299 | |
| B | SER299 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17582436 |
| Chain | Residue | Details |
| A | ASP145 | |
| A | SER299 | |
| A | HIS352 | |
| A | THR412 | |
| B | ASP145 | |
| B | SER299 | |
| B | HIS352 | |
| B | THR412 |
