5KSH
Crystal structure of penicillin-binding protein 2 from Neisseria gonorrhoeae containing an A501T mutation associated with cephalosporin resistance
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 | 0008233 | molecular_function | peptidase activity |
| 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 | 0016787 | molecular_function | hydrolase activity |
| A | 0043093 | biological_process | FtsZ-dependent cytokinesis |
| A | 0046677 | biological_process | response to antibiotic |
| 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 | 0008233 | molecular_function | peptidase activity |
| 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 | 0016787 | molecular_function | hydrolase activity |
| B | 0043093 | biological_process | FtsZ-dependent cytokinesis |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0051301 | biological_process | cell division |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 601 |
| Chain | Residue |
| A | GLU190 |
| A | GLY191 |
| A | ARG298 |
| A | ASN299 |
| A | PRO397 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 602 |
| Chain | Residue |
| A | ARG67 |
| A | ARG211 |
| B | ARG408 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 603 |
| Chain | Residue |
| A | PRO289 |
| A | GLY290 |
| A | ARG291 |
| A | ARG288 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 604 |
| Chain | Residue |
| A | SER294 |
| A | ARG297 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 605 |
| Chain | Residue |
| A | VAL390 |
| A | ARG391 |
| A | HIS393 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 606 |
| Chain | Residue |
| A | ARG81 |
| A | LYS451 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 601 |
| Chain | Residue |
| B | GLU190 |
| B | GLY191 |
| B | ARG297 |
| B | ARG298 |
| B | ASN299 |
| B | THR303 |
| B | PRO397 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 602 |
| Chain | Residue |
| B | TYR284 |
| B | ASP285 |
| B | ARG288 |
| B | ARG291 |
| B | ALA292 |
| B | GLN296 |
| B | SO4608 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 603 |
| Chain | Residue |
| B | SER342 |
| B | LYS361 |
| B | ARG411 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 604 |
| Chain | Residue |
| A | GLN457 |
| B | ARG288 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 605 |
| Chain | Residue |
| B | ARG288 |
| B | PRO289 |
| B | GLY290 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 606 |
| Chain | Residue |
| B | SER294 |
| B | ARG297 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 607 |
| Chain | Residue |
| A | GLU59 |
| A | GLN60 |
| B | ARG345 |
| B | ASN406 |
| B | ARG409 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 608 |
| Chain | Residue |
| A | PRO446 |
| B | ARG291 |
| B | GOL602 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 609 |
| Chain | Residue |
| B | ASP293 |
| B | SER294 |
| B | ARG297 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_02080","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
