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 | 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 | 0016757 | molecular_function | glycosyltransferase activity |
A | 0046677 | biological_process | response to antibiotic |
A | 0071555 | biological_process | cell wall organization |
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 | 0016757 | molecular_function | glycosyltransferase activity |
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 | ACT_SITE: Proton donor; for transglycosylase activity => ECO:0000250|UniProtKB:P02919 |
Chain | Residue | Details |
A | GLU86 | |
B | GLU86 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Acyl-ester intermediate; for transpeptidase activity => ECO:0000250|UniProtKB:P02919 |
Chain | Residue | Details |
A | SER452 | |
B | SER452 |