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 | 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 | 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 | 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 | 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 | ACT_SITE: Acyl-ester intermediate => ECO:0000255|HAMAP-Rule:MF_02080 |
Chain | Residue | Details |
A | SER310 | |
B | SER310 |