Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008800 | molecular_function | beta-lactamase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0017001 | biological_process | antibiotic catabolic process |
A | 0042597 | cellular_component | periplasmic space |
A | 0046677 | biological_process | response to antibiotic |
A | 0046872 | molecular_function | metal ion binding |
B | 0008270 | molecular_function | zinc ion binding |
B | 0008800 | molecular_function | beta-lactamase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0017001 | biological_process | antibiotic catabolic process |
B | 0042597 | cellular_component | periplasmic space |
B | 0046677 | biological_process | response to antibiotic |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 401 |
Chain | Residue |
A | HIS116 |
A | HIS118 |
A | HIS196 |
A | MCO1410 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 402 |
Chain | Residue |
A | ASP120 |
A | HIS121 |
A | HIS263 |
A | MCO1410 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 401 |
Chain | Residue |
B | HIS118 |
B | HIS196 |
B | MCO2410 |
B | HIS116 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 402 |
Chain | Residue |
B | ASP120 |
B | HIS121 |
B | HIS263 |
B | MCO2410 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 2 |
Chain | Residue |
A | ARG172 |
A | VAL179 |
A | ILE180 |
A | THR181 |
A | HOH1754 |
A | HOH1760 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 3 |
Chain | Residue |
B | ARG172 |
B | VAL179 |
B | ILE180 |
B | THR181 |
B | HOH2483 |
B | HOH2645 |
B | HOH2720 |
B | HOH2732 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 4 |
Chain | Residue |
A | ARG102 |
A | ASN210 |
A | HOH1479 |
A | HOH1723 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 5 |
Chain | Residue |
A | ARG252 |
A | LYS297 |
B | ARG209 |
B | ALA275 |
B | ARG276 |
B | ALA289 |
B | GLY290 |
B | ALA291 |
B | HOH2551 |
B | HOH2571 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 6 |
Chain | Residue |
A | ARG252 |
A | HOH1713 |
B | ARG209 |
B | ASN210 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 7 |
Chain | Residue |
A | ARG209 |
A | ALA275 |
A | ARG276 |
A | ALA289 |
A | GLY290 |
A | ALA291 |
A | HOH1527 |
A | HOH1591 |
B | ARG252 |
B | LYS297 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 8 |
Chain | Residue |
A | ARG209 |
B | ARG252 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 9 |
Chain | Residue |
B | ARG102 |
B | GLY211 |
B | HOH2574 |
site_id | BC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE MCO A 1410 |
Chain | Residue |
A | TYR33 |
A | TRP39 |
A | ASP120 |
A | HIS196 |
A | SER225 |
A | PRO227 |
A | HIS263 |
A | ZN401 |
A | ZN402 |
A | HOH1496 |
A | HOH1649 |
A | HOH1765 |
A | HOH1767 |
site_id | BC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE MCO B 2410 |
Chain | Residue |
B | TYR33 |
B | TRP39 |
B | ASP120 |
B | HIS196 |
B | SER225 |
B | PRO227 |
B | HIS263 |
B | ZN401 |
B | ZN402 |
B | HOH2531 |
B | HOH2614 |
B | HOH2702 |
B | HOH2725 |
site_id | BC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 1 |
Chain | Residue |
A | ALA249 |
A | ARG252 |
A | GLU304 |
A | HOH1498 |
A | HOH1542 |
A | HOH1564 |
A | HOH1647 |
B | ARG276 |
Functional Information from PROSITE/UniProt
site_id | PS00743 |
Number of Residues | 21 |
Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. LlSHaHADhaGPvaelkrrtG |
Chain | Residue | Details |
A | LEU113-GLY133 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS116 | |
B | HIS196 | |
A | HIS118 | |
A | ASP120 | |
A | HIS121 | |
A | HIS196 | |
B | HIS116 | |
B | HIS118 | |
B | ASP120 | |
B | HIS121 | |
Chain | Residue | Details |
A | ASP220 | |
B | ASP220 | |
Chain | Residue | Details |
A | HIS263 | |
B | HIS263 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qh5 |
Chain | Residue | Details |
A | ASP120 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qh5 |
Chain | Residue | Details |
B | ASP120 | |
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 258 |
Chain | Residue | Details |
A | HIS116 | metal ligand |
A | HIS118 | metal ligand |
A | ASP120 | metal ligand |
A | HIS121 | metal ligand |
A | HIS196 | metal ligand |
A | TYR229 | electrostatic stabiliser, hydrogen bond donor |
A | HIS263 | metal ligand |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 258 |
Chain | Residue | Details |
B | HIS116 | metal ligand |
B | HIS118 | metal ligand |
B | ASP120 | metal ligand |
B | HIS121 | metal ligand |
B | HIS196 | metal ligand |
B | TYR229 | electrostatic stabiliser, hydrogen bond donor |
B | HIS263 | metal ligand |