3A3D
Crystal structure of penicillin binding protein 4 (dacB) from Haemophilus influenzae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000270 | biological_process | peptidoglycan metabolic process |
| A | 0004185 | molecular_function | serine-type carboxypeptidase activity |
| 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 | 0016787 | molecular_function | hydrolase activity |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0051301 | biological_process | cell division |
| A | 0071555 | biological_process | cell wall organization |
| B | 0000270 | biological_process | peptidoglycan metabolic process |
| B | 0004185 | molecular_function | serine-type carboxypeptidase activity |
| 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 | 0016787 | molecular_function | hydrolase activity |
| B | 0042597 | cellular_component | periplasmic space |
| 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 | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 480 |
| Chain | Residue |
| A | ASN139 |
| A | ASP141 |
| A | LYS278 |
| A | HOH737 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 481 |
| Chain | Residue |
| A | HOH525 |
| A | HOH783 |
| A | HOH913 |
| A | GLN254 |
| A | ASN255 |
| A | THR256 |
| A | ASP257 |
| A | HOH486 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 482 |
| Chain | Residue |
| A | MET390 |
| A | ASN416 |
| A | MET434 |
| A | THR435 |
| A | LYS441 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1 |
| Chain | Residue |
| B | ARG120 |
| B | GLN267 |
| B | LYS270 |
| B | HOH782 |
| B | HOH817 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Acyl-ester intermediate => ECO:0000250|UniProtKB:P39844 |
| Chain | Residue | Details |
| A | SER69 | |
| B | SER69 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P39844 |
| Chain | Residue | Details |
| A | LYS72 | |
| B | LYS72 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P39844 |
| Chain | Residue | Details |
| A | SER310 | |
| B | SER310 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS420 | |
| B | LYS420 |
