4KQO
Crystal structure of penicillin-binding protein 3 from pseudomonas aeruginosa in complex with piperacillin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000917 | biological_process | division septum assembly |
| A | 0004180 | molecular_function | carboxypeptidase activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006508 | biological_process | proteolysis |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0008658 | molecular_function | penicillin binding |
| A | 0008955 | molecular_function | peptidoglycan glycosyltransferase activity |
| A | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0043093 | biological_process | FtsZ-dependent cytokinesis |
| A | 0051301 | biological_process | cell division |
| A | 0071555 | biological_process | cell wall organization |
| B | 0000917 | biological_process | division septum assembly |
| B | 0004180 | molecular_function | carboxypeptidase activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006508 | biological_process | proteolysis |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0008658 | molecular_function | penicillin binding |
| B | 0008955 | molecular_function | peptidoglycan glycosyltransferase activity |
| B | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0043093 | biological_process | FtsZ-dependent cytokinesis |
| B | 0051301 | biological_process | cell division |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE JPP A 601 |
| Chain | Residue |
| A | SER294 |
| A | ALA488 |
| A | ARG489 |
| A | TYR498 |
| A | GLY534 |
| A | HOH732 |
| A | HOH829 |
| A | HOH847 |
| A | HOH849 |
| A | TYR328 |
| A | VAL333 |
| A | SER349 |
| A | ASN351 |
| A | TYR409 |
| A | SER485 |
| A | GLY486 |
| A | THR487 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 602 |
| Chain | Residue |
| A | GLY247 |
| A | SER248 |
| A | ARG284 |
| A | PHE290 |
| A | ASP525 |
| A | HOH704 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 603 |
| Chain | Residue |
| A | SER435 |
| A | MET436 |
| A | THR437 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE JPP B 601 |
| Chain | Residue |
| B | SER294 |
| B | TYR328 |
| B | VAL333 |
| B | SER349 |
| B | ASN351 |
| B | TYR409 |
| B | LYS484 |
| B | SER485 |
| B | GLY486 |
| B | THR487 |
| B | ARG489 |
| B | TYR498 |
| B | HOH706 |
| B | HOH762 |
| B | HOH819 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 602 |
| Chain | Residue |
| B | GLY247 |
| B | SER248 |
| B | ARG284 |
| B | PHE290 |
| B | VAL523 |
| B | ASP525 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IMD B 603 |
| Chain | Residue |
| B | ARG551 |
| B | ASN554 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 604 |
| Chain | Residue |
| B | LYS490 |
| B | VAL491 |
| B | ARG504 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 605 |
| Chain | Residue |
| B | ARG152 |
| B | ARG273 |
| B | ARG274 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Acyl-ester intermediate => ECO:0000255|HAMAP-Rule:MF_02080 |
| Chain | Residue | Details |
| A | SER294 | |
| B | SER294 |
