2Y55
Unexpected tricovalent binding mode of boronic acids within the active site of a penicillin binding protein
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000270 | biological_process | peptidoglycan metabolic process |
A | 0004180 | molecular_function | carboxypeptidase activity |
A | 0004185 | molecular_function | serine-type carboxypeptidase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0006508 | biological_process | proteolysis |
A | 0008360 | biological_process | regulation of cell shape |
A | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
A | 0009252 | biological_process | peptidoglycan biosynthetic process |
A | 0046677 | biological_process | response to antibiotic |
A | 0071555 | biological_process | cell wall organization |
B | 0000270 | biological_process | peptidoglycan metabolic process |
B | 0004180 | molecular_function | carboxypeptidase activity |
B | 0004185 | molecular_function | serine-type carboxypeptidase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0006508 | biological_process | proteolysis |
B | 0008360 | biological_process | regulation of cell shape |
B | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
B | 0009252 | biological_process | peptidoglycan biosynthetic process |
B | 0046677 | biological_process | response to antibiotic |
B | 0071555 | biological_process | cell wall organization |
C | 0000270 | biological_process | peptidoglycan metabolic process |
C | 0004180 | molecular_function | carboxypeptidase activity |
C | 0004185 | molecular_function | serine-type carboxypeptidase activity |
C | 0005576 | cellular_component | extracellular region |
C | 0006508 | biological_process | proteolysis |
C | 0008360 | biological_process | regulation of cell shape |
C | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
C | 0009252 | biological_process | peptidoglycan biosynthetic process |
C | 0046677 | biological_process | response to antibiotic |
C | 0071555 | biological_process | cell wall organization |
D | 0000270 | biological_process | peptidoglycan metabolic process |
D | 0004180 | molecular_function | carboxypeptidase activity |
D | 0004185 | molecular_function | serine-type carboxypeptidase activity |
D | 0005576 | cellular_component | extracellular region |
D | 0006508 | biological_process | proteolysis |
D | 0008360 | biological_process | regulation of cell shape |
D | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
D | 0009252 | biological_process | peptidoglycan biosynthetic process |
D | 0046677 | biological_process | response to antibiotic |
D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE FP5 A 500 |
Chain | Residue |
A | ALA48 |
A | ACN1473 |
A | SER49 |
A | LYS52 |
A | SER298 |
A | ASN300 |
A | LYS410 |
A | THR411 |
A | GLY412 |
A | THR413 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 1467 |
Chain | Residue |
A | ASP281 |
A | HIS282 |
A | THR283 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 1468 |
Chain | Residue |
A | ALA234 |
A | ARG236 |
A | HOH2079 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1469 |
Chain | Residue |
A | SER131 |
A | GLU132 |
A | ARG133 |
A | LEU134 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 1470 |
Chain | Residue |
A | GLY159 |
A | GLU160 |
A | ARG161 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 1471 |
Chain | Residue |
A | GLU188 |
A | HIS247 |
A | GLU251 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG A 1472 |
Chain | Residue |
A | VAL406 |
A | HIS462 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACN A 1473 |
Chain | Residue |
A | TYR147 |
A | THR413 |
A | MET414 |
A | FP5500 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 A 1474 |
Chain | Residue |
A | ARG161 |
site_id | BC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE FP5 B 500 |
Chain | Residue |
B | ALA48 |
B | SER49 |
B | LYS52 |
B | SER298 |
B | ASN300 |
B | SER347 |
B | GLY348 |
B | LEU349 |
B | LYS410 |
B | THR411 |
B | GLY412 |
B | THR413 |
B | ACN1471 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 1467 |
Chain | Residue |
B | ASP281 |
B | HIS282 |
B | THR283 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 1468 |
Chain | Residue |
B | ALA234 |
B | ARG236 |
B | HOH2068 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 1469 |
Chain | Residue |
B | SER131 |
B | GLU132 |
B | ARG133 |
B | LEU134 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 1470 |
Chain | Residue |
B | HIS158 |
B | GLY159 |
B | GLU160 |
B | ARG161 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACN B 1471 |
Chain | Residue |
B | THR413 |
B | FP5500 |
site_id | BC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FP5 C 500 |
Chain | Residue |
C | ALA48 |
C | SER49 |
C | LYS52 |
C | SER298 |
C | ASN300 |
C | GLY348 |
C | LYS410 |
C | GLY412 |
C | THR413 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 1467 |
Chain | Residue |
C | ASP281 |
C | HIS282 |
C | THR283 |
C | HOH2064 |
site_id | BC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 C 1468 |
Chain | Residue |
C | ARG236 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 1469 |
Chain | Residue |
C | SER131 |
C | ARG133 |
C | LEU134 |
site_id | CC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 1470 |
Chain | Residue |
C | GLY159 |
C | GLU160 |
C | ARG161 |
site_id | CC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ACN C 1471 |
Chain | Residue |
C | THR413 |
site_id | CC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FP5 D 500 |
Chain | Residue |
D | SER49 |
D | LYS52 |
D | SER298 |
D | ASN300 |
D | LYS410 |
D | THR411 |
D | THR413 |
D | MET414 |
D | ACN1473 |
site_id | CC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 1467 |
Chain | Residue |
D | ASP281 |
D | HIS282 |
D | THR283 |
D | HOH2034 |
site_id | CC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 D 1468 |
Chain | Residue |
D | ALA234 |
D | ARG236 |
site_id | CC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 1469 |
Chain | Residue |
D | GLU132 |
D | ARG133 |
D | LEU134 |
D | SER131 |
site_id | CC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 1470 |
Chain | Residue |
D | GLY159 |
D | GLU160 |
D | ARG161 |
site_id | CC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG D 1471 |
Chain | Residue |
D | GLU188 |
D | HIS247 |
D | GLU251 |
site_id | DC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MG D 1472 |
Chain | Residue |
D | HIS462 |
site_id | DC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACN D 1473 |
Chain | Residue |
D | ASP142 |
D | TYR147 |
D | LEU349 |
D | MET414 |
D | FP5500 |
site_id | DC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACN D 1474 |
Chain | Residue |
D | THR127 |
D | GLY318 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Acyl-ester intermediate |
Chain | Residue | Details |
A | SER49 | |
B | SER49 | |
C | SER49 | |
D | SER49 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | LYS52 | |
B | LYS52 | |
C | LYS52 | |
D | LYS52 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000250 |
Chain | Residue | Details |
A | SER298 | |
B | SER298 | |
C | SER298 | |
D | SER298 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS410 | |
B | LYS410 | |
C | LYS410 | |
D | LYS410 |