4KQQ
CRYSTAL STRUCTURE OF PENICILLIN-BINDING PROTEIN 3 FROM PSEUDOMONAS AERUGINOSA IN COMPLEX WITH (5S)-Penicilloic Acid
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 | 20 |
| Details | BINDING SITE FOR RESIDUE VPP A 601 |
| Chain | Residue |
| A | SER294 |
| A | GLY486 |
| A | THR487 |
| A | ARG489 |
| A | TYR498 |
| A | TYR503 |
| A | PHE533 |
| A | GLY534 |
| A | GLY535 |
| A | IMD605 |
| A | HOH733 |
| A | LYS297 |
| A | HOH768 |
| A | VAL333 |
| A | SER349 |
| A | ASN351 |
| A | THR404 |
| A | TYR407 |
| A | TYR409 |
| A | SER485 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 602 |
| Chain | Residue |
| A | LYS311 |
| A | PRO312 |
| A | SER313 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 603 |
| Chain | Residue |
| A | GLY247 |
| A | SER248 |
| A | ARG284 |
| A | VAL523 |
| A | ASP525 |
| A | HOH705 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 604 |
| Chain | Residue |
| A | TYR268 |
| A | ASN269 |
| A | ASN272 |
| A | ASN275 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IMD A 605 |
| Chain | Residue |
| A | TYR328 |
| A | THR329 |
| A | THR404 |
| A | TYR407 |
| A | VPP601 |
| A | HOH810 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE VPP B 601 |
| Chain | Residue |
| B | SER294 |
| B | LYS297 |
| B | TYR328 |
| B | VAL333 |
| B | SER349 |
| B | ASN351 |
| B | THR404 |
| B | TYR407 |
| B | TYR409 |
| B | SER485 |
| B | GLY486 |
| B | THR487 |
| B | ARG489 |
| B | TYR498 |
| B | TYR503 |
| B | PHE533 |
| B | GLY534 |
| B | GLY535 |
| B | HOH730 |
| B | HOH757 |
| B | HOH771 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 602 |
| Chain | Residue |
| B | VAL491 |
| B | ARG504 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 603 |
| Chain | Residue |
| B | ARG499 |
| B | GLU500 |
| B | ASN501 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 604 |
| Chain | Residue |
| B | GLY247 |
| B | SER248 |
| B | ARG284 |
| B | PHE290 |
| B | VAL523 |
| B | ASP525 |
| B | HOH718 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 605 |
| Chain | Residue |
| B | ASN501 |
| B | PRO527 |
| B | SER528 |
| B | TYR532 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 606 |
| Chain | Residue |
| B | GLU159 |
| B | GLN265 |
| B | PRO266 |
| B | THR267 |
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 |
