5U2G
2.6 Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| 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 | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0071555 | biological_process | cell wall organization |
| B | 0003824 | molecular_function | catalytic activity |
| 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 | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 901 |
| Chain | Residue |
| A | LYS204 |
| A | ARG221 |
| A | ARG228 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 902 |
| Chain | Residue |
| A | ARG384 |
| A | SER385 |
| A | ASN386 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 903 |
| Chain | Residue |
| A | HOH1055 |
| A | ILE478 |
| A | SER479 |
| A | ARG517 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 904 |
| Chain | Residue |
| A | TRP714 |
| A | ARG715 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 905 |
| Chain | Residue |
| A | ASP296 |
| A | GLU427 |
| A | ASP786 |
| A | LYS787 |
| A | HOH1053 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 906 |
| Chain | Residue |
| A | ARG561 |
| A | HOH1056 |
| A | HOH1116 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 A 907 |
| Chain | Residue |
| A | ARG274 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 A 908 |
| Chain | Residue |
| A | ARG335 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 910 |
| Chain | Residue |
| A | THR731 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 911 |
| Chain | Residue |
| A | ARG275 |
| A | ILE577 |
| A | ILE578 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 912 |
| Chain | Residue |
| A | GLN297 |
| A | GLN301 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 914 |
| Chain | Residue |
| A | SER785 |
| A | LYS787 |
| A | PRO788 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 901 |
| Chain | Residue |
| B | LYS204 |
| B | ARG221 |
| B | ARG228 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 902 |
| Chain | Residue |
| B | ARG384 |
| B | SER385 |
| B | ASN386 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 903 |
| Chain | Residue |
| B | ASP296 |
| B | GLU427 |
| B | ASP786 |
| B | LYS787 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 904 |
| Chain | Residue |
| B | ILE478 |
| B | SER479 |
| B | ARG517 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 905 |
| Chain | Residue |
| B | TRP714 |
| B | ARG715 |
| B | HOH1109 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 906 |
| Chain | Residue |
| B | TYR702 |
| B | ARG722 |
| B | HOH1003 |
| site_id | AE1 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 B 907 |
| Chain | Residue |
| B | ARG335 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 908 |
| Chain | Residue |
| B | ARG561 |
| B | LEU572 |
| B | HOH1043 |
| B | HOH1122 |
| site_id | AE3 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 910 |
| Chain | Residue |
| B | THR731 |
| site_id | AE4 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 911 |
| Chain | Residue |
| B | ARG275 |
| B | ILE577 |
| B | ILE578 |
| site_id | AE5 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 912 |
| Chain | Residue |
| B | TYR263 |
| B | GLN297 |
| B | GLN301 |
| site_id | AE6 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 913 |
| Chain | Residue |
| B | LYS587 |
| B | LEU589 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Acyl-ester intermediate; for transpeptidase activity","evidences":[{"source":"UniProtKB","id":"P02919","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
