4HES
Structure of a Beta-Lactamase Class A-like Protein from Veillonella parvula.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008800 | molecular_function | beta-lactamase activity |
A | 0017001 | biological_process | antibiotic catabolic process |
A | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
A | 0046677 | biological_process | response to antibiotic |
B | 0008800 | molecular_function | beta-lactamase activity |
B | 0017001 | biological_process | antibiotic catabolic process |
B | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
B | 0046677 | biological_process | response to antibiotic |
C | 0008800 | molecular_function | beta-lactamase activity |
C | 0017001 | biological_process | antibiotic catabolic process |
C | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
C | 0046677 | biological_process | response to antibiotic |
D | 0008800 | molecular_function | beta-lactamase activity |
D | 0017001 | biological_process | antibiotic catabolic process |
D | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
D | 0046677 | biological_process | response to antibiotic |
E | 0008800 | molecular_function | beta-lactamase activity |
E | 0017001 | biological_process | antibiotic catabolic process |
E | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
E | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 301 |
Chain | Residue |
A | SER56 |
A | SER117 |
A | THR218 |
A | GLY219 |
A | SER220 |
A | HOH474 |
A | HOH493 |
A | HOH673 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 302 |
Chain | Residue |
A | HIS68 |
A | GLN74 |
A | ALA136 |
A | ARG137 |
A | HOH431 |
A | HOH585 |
A | HOH696 |
A | TYR65 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 303 |
Chain | Residue |
A | ASP202 |
A | FMT304 |
A | HOH419 |
B | ASP202 |
B | FMT304 |
B | HOH414 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT A 304 |
Chain | Residue |
A | ASP202 |
A | PHE206 |
A | LYS253 |
A | NA303 |
B | FMT304 |
B | HOH460 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 301 |
Chain | Residue |
B | SER56 |
B | SER117 |
B | THR218 |
B | GLY219 |
B | SER220 |
B | HOH489 |
B | HOH722 |
B | HOH730 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 302 |
Chain | Residue |
B | ARG189 |
B | ASN193 |
B | HOH422 |
B | HOH556 |
B | HOH565 |
C | ARG88 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 303 |
Chain | Residue |
A | ARG189 |
A | ASN193 |
B | ARG88 |
B | HOH407 |
B | HOH560 |
B | HOH598 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT B 304 |
Chain | Residue |
A | NA303 |
A | FMT304 |
A | HOH464 |
B | ASP202 |
B | PHE206 |
B | LYS253 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL C 301 |
Chain | Residue |
C | SER56 |
C | SER117 |
C | THR218 |
C | GLY219 |
C | SER220 |
C | HOH466 |
C | HOH469 |
C | HOH626 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 302 |
Chain | Residue |
C | ARG88 |
C | GLN96 |
C | GLU97 |
C | LEU98 |
C | VAL99 |
C | HOH570 |
D | ARG111 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT C 303 |
Chain | Residue |
C | ASP202 |
C | PHE206 |
C | LYS253 |
D | FMT305 |
D | NA306 |
D | HOH533 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL D 301 |
Chain | Residue |
D | SER56 |
D | SER117 |
D | PHE200 |
D | THR218 |
D | GLY219 |
D | SER220 |
D | HOH462 |
D | HOH476 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL D 302 |
Chain | Residue |
A | ARG88 |
D | ARG189 |
D | ASN193 |
D | HOH410 |
D | HOH525 |
D | HOH638 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL D 303 |
Chain | Residue |
D | ARG88 |
D | HOH421 |
D | HOH522 |
D | HOH608 |
E | ARG189 |
E | ASN193 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL D 304 |
Chain | Residue |
D | SER103 |
C | HIS102 |
C | SER103 |
C | HOH446 |
D | HIS102 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT D 305 |
Chain | Residue |
C | FMT303 |
C | HOH479 |
D | ASP202 |
D | PHE206 |
D | LYS253 |
D | NA306 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA D 306 |
Chain | Residue |
C | ASP202 |
C | FMT303 |
C | HOH414 |
D | ASP202 |
D | FMT305 |
D | HOH464 |
site_id | BC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL E 301 |
Chain | Residue |
E | SER56 |
E | SER117 |
E | PHE200 |
E | THR218 |
E | GLY219 |
E | SER220 |
E | HOH460 |
E | HOH581 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL E 302 |
Chain | Residue |
C | ARG189 |
C | ASN193 |
E | ARG88 |
E | HOH412 |
E | HOH528 |
E | HOH530 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL E 303 |
Chain | Residue |
E | TYR65 |
E | VAL128 |
E | LEU129 |
E | ASN133 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL E 304 |
Chain | Residue |
E | GLU37 |
E | GLU39 |
E | LYS176 |
E | HOH479 |
E | HOH554 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL E 305 |
Chain | Residue |
E | ILE5 |
E | LYS8 |
E | GLU11 |
site_id | CC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL E 306 |
Chain | Residue |
E | ARG137 |
E | HIS177 |
E | ARG184 |
E | HOH475 |
E | HOH671 |
site_id | CC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA E 307 |
Chain | Residue |
E | ASP202 |
E | ASP202 |
E | FMT308 |
E | FMT308 |
E | HOH437 |
E | HOH437 |
site_id | CC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT E 308 |
Chain | Residue |
E | ASP202 |
E | PHE206 |
E | LYS253 |
E | NA307 |
E | NA307 |
E | HOH471 |