2XLN
Crystal structure of a complex between Actinomadura R39 DD-peptidase and a boronate inhibitor
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 | 12 |
| Details | BINDING SITE FOR RESIDUE EWA A 500 |
| Chain | Residue |
| A | ALA48 |
| B | ALA175 |
| B | GLU176 |
| B | GLU178 |
| A | SER49 |
| A | LYS52 |
| A | TYR147 |
| A | SER298 |
| A | ASN300 |
| A | LEU349 |
| A | THR413 |
| A | HOH2191 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE EWA B 500 |
| Chain | Residue |
| B | ALA48 |
| B | SER49 |
| B | TYR147 |
| B | SER298 |
| B | ASN300 |
| B | LEU349 |
| B | GLY412 |
| B | THR413 |
| B | MET414 |
| B | HOH2161 |
| B | HOH2203 |
| B | HOH2205 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE EWA C 500 |
| Chain | Residue |
| C | ALA48 |
| C | SER49 |
| C | ASP142 |
| C | TYR147 |
| C | SER298 |
| C | ASN300 |
| C | LEU349 |
| C | GLY412 |
| C | THR413 |
| C | MET414 |
| C | HOH2201 |
| C | HOH2202 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EWA D 500 |
| Chain | Residue |
| D | ALA48 |
| D | SER49 |
| D | TYR147 |
| D | SER298 |
| D | ASN300 |
| D | GLY348 |
| D | LEU349 |
| D | GLY412 |
| D | THR413 |
| D | HOH2177 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 601 |
| Chain | Residue |
| A | HIS282 |
| A | THR283 |
| A | HOH2209 |
| A | HOH2210 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 602 |
| Chain | Residue |
| A | ALA234 |
| A | ARG236 |
| A | HOH2211 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 603 |
| Chain | Residue |
| A | SER131 |
| A | GLU132 |
| A | ARG133 |
| A | LEU134 |
| A | HOH2212 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 604 |
| Chain | Residue |
| A | GLU160 |
| A | ARG161 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO A 610 |
| Chain | Residue |
| A | GLU188 |
| A | HIS247 |
| A | GLU251 |
| A | HOH2213 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 601 |
| Chain | Residue |
| B | HIS282 |
| B | THR283 |
| B | HOH2057 |
| B | HOH2152 |
| B | HOH2154 |
| B | HOH2155 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 602 |
| Chain | Residue |
| B | ALA234 |
| B | ARG236 |
| B | HOH2206 |
| B | HOH2207 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 603 |
| Chain | Residue |
| B | SER131 |
| B | GLU132 |
| B | ARG133 |
| B | LEU134 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 604 |
| Chain | Residue |
| B | GLY159 |
| B | GLU160 |
| B | ARG161 |
| B | HOH2092 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 605 |
| Chain | Residue |
| B | ARG1 |
| B | ARG455 |
| B | TYR459 |
| D | ARG1 |
| D | LEU2 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 601 |
| Chain | Residue |
| C | ASP281 |
| C | HIS282 |
| C | THR283 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 602 |
| Chain | Residue |
| C | ARG236 |
| C | HOH2203 |
| C | HOH2204 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 603 |
| Chain | Residue |
| C | SER131 |
| C | GLU132 |
| C | ARG133 |
| C | LEU134 |
| C | HOH2205 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 604 |
| Chain | Residue |
| C | GLY159 |
| C | GLU160 |
| C | ARG161 |
| C | HOH2086 |
| C | HOH2087 |
| C | HIS158 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 601 |
| Chain | Residue |
| D | ASP281 |
| D | HIS282 |
| D | THR283 |
| D | HOH2046 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 602 |
| Chain | Residue |
| D | ALA234 |
| D | ARG236 |
| D | HOH2188 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 603 |
| Chain | Residue |
| D | SER131 |
| D | ARG133 |
| D | LEU134 |
| D | HOH2190 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 604 |
| Chain | Residue |
| D | GLY159 |
| D | GLU160 |
| D | ARG161 |
| D | HOH2084 |
| site_id | CC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CO D 610 |
| Chain | Residue |
| D | GLU188 |
| D | HIS247 |
| D | GLU251 |
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 |
