3ITA
Crystal structure of Penicillin-Binding Protein 6 (PBP6) from E. coli in acyl-enzyme complex with ampicillin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000270 | biological_process | peptidoglycan metabolic process |
| 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 | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0000270 | biological_process | peptidoglycan metabolic process |
| 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 | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0009410 | biological_process | response to xenobiotic stimulus |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0042803 | molecular_function | protein homodimerization activity |
| C | 0000270 | biological_process | peptidoglycan metabolic process |
| C | 0004180 | molecular_function | carboxypeptidase activity |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006508 | biological_process | proteolysis |
| C | 0008360 | biological_process | regulation of cell shape |
| C | 0008658 | molecular_function | penicillin binding |
| C | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
| C | 0009252 | biological_process | peptidoglycan biosynthetic process |
| C | 0009410 | biological_process | response to xenobiotic stimulus |
| C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| C | 0042803 | molecular_function | protein homodimerization activity |
| D | 0000270 | biological_process | peptidoglycan metabolic process |
| D | 0004180 | molecular_function | carboxypeptidase activity |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006508 | biological_process | proteolysis |
| D | 0008360 | biological_process | regulation of cell shape |
| D | 0008658 | molecular_function | penicillin binding |
| D | 0009002 | molecular_function | serine-type D-Ala-D-Ala carboxypeptidase activity |
| D | 0009252 | biological_process | peptidoglycan biosynthetic process |
| D | 0009410 | biological_process | response to xenobiotic stimulus |
| D | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE AIX A 500 |
| Chain | Residue |
| A | ALA39 |
| A | SER40 |
| A | ARG194 |
| A | THR210 |
| A | GLY211 |
| A | THR212 |
| A | ARG244 |
| A | HOH723 |
| A | HOH754 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 353 |
| Chain | Residue |
| A | ARG242 |
| A | HOH455 |
| A | HOH487 |
| B | GLU183 |
| B | ARG190 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 353 |
| Chain | Residue |
| A | ARG190 |
| B | ARG194 |
| B | THR210 |
| B | GLY211 |
| B | THR212 |
| B | ARG244 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 354 |
| Chain | Residue |
| B | GLN300 |
| B | ASN303 |
| B | HOH825 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 353 |
| Chain | Residue |
| C | THR240 |
| C | ARG242 |
| C | HOH365 |
| C | HOH366 |
| D | TRP199 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 354 |
| Chain | Residue |
| C | THR210 |
| C | GLY211 |
| C | THR212 |
| C | ARG244 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 355 |
| Chain | Residue |
| C | GLU183 |
| C | TRP199 |
| D | THR240 |
| D | ARG242 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE AIC D 501 |
| Chain | Residue |
| D | PRO264 |
| D | PHE271 |
| D | LEU304 |
| D | LYS305 |
| D | ALA306 |
| D | HOH680 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Acyl-ester intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| A | SER106 | |
| A | SER40 | |
| A | LYS43 | |
| A | GLN144 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| B | SER106 | |
| B | SER40 | |
| B | LYS43 | |
| B | GLN144 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| C | SER106 | |
| C | SER40 | |
| C | LYS43 | |
| C | GLN144 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| D | SER106 | |
| D | SER40 | |
| D | LYS43 | |
| D | GLN144 |
