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 | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 401 |
Chain | Residue |
A | HIS86 |
A | HIS88 |
A | HIS149 |
A | HOH726 |
A | HOH812 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 402 |
Chain | Residue |
B | HOH816 |
B | HIS86 |
B | HIS88 |
B | HIS149 |
B | HOH785 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 501 |
Chain | Residue |
A | SER172 |
A | THR173 |
A | SER174 |
A | GLY211 |
A | GLU212 |
A | HOH773 |
A | HOH845 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 502 |
Chain | Residue |
B | SER172 |
B | THR173 |
B | SER174 |
B | GLY211 |
B | GLU212 |
B | HOH706 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 503 |
Chain | Residue |
A | LYS65 |
A | GLU69 |
A | ARG101 |
A | ILE203 |
A | LYS216 |
A | HOH744 |
A | HOH806 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 504 |
Chain | Residue |
B | LYS134 |
B | LYS139 |
B | ARG199 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 505 |
Chain | Residue |
A | SER168 |
A | LYS171 |
A | HIS210 |
A | HOH750 |
A | HOH765 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 506 |
Chain | Residue |
B | SER168 |
B | LYS171 |
B | GLY209 |
B | HIS210 |
B | HOH732 |
B | HOH743 |
B | HOH850 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACY B 601 |
Chain | Residue |
B | ASP60 |
B | ASP61 |
B | LYS62 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACY A 602 |
Chain | Residue |
A | LYS99 |
A | GLU121 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ACY A 603 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACY B 604 |
Chain | Residue |
B | LYS99 |
B | GLU121 |
B | GLU122 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACY B 605 |
Chain | Residue |
B | ASN162 |
B | ASN202 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACY B 606 |
Chain | Residue |
B | ALA175 |
B | LYS176 |
B | ASP177 |
B | HOH854 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACY A 607 |
Chain | Residue |
A | ASP60 |
A | ASP61 |
A | LYS62 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACY A 608 |
Chain | Residue |
A | ALA175 |
A | LYS176 |
A | ASP177 |
A | HOH873 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 701 |
Chain | Residue |
A | ASN137 |
A | LYS139 |
A | GLN160 |
A | HOH740 |
site_id | BC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 702 |
Chain | Residue |
A | ALA182 |
A | ASP183 |
A | ALA184 |
A | TYR185 |
A | HOH832 |
A | HOH874 |
B | LYS227 |
site_id | CC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 703 |
Chain | Residue |
B | THR29 |
B | ASN42 |
B | GLY211 |
B | GLU212 |
B | VAL213 |
B | HOH720 |
B | HOH723 |
B | HOH894 |
Functional Information from PROSITE/UniProt
site_id | PS00743 |
Number of Residues | 20 |
Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IiTHaHADhiGGiktlker.G |
Chain | Residue | Details |
A | ILE83-GLY102 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS86 | |
A | HIS88 | |
A | HIS149 | |
B | HIS86 | |
B | HIS88 | |
B | HIS149 | |
Chain | Residue | Details |
A | ASP90 | |
A | SER168 | |
A | HIS210 | |
B | ASP90 | |
B | SER168 | |
B | HIS210 | |
Chain | Residue | Details |
A | LYS171 | |
B | LYS171 | |
Chain | Residue | Details |
A | ASN180 | |
B | ASN180 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
A | ASP90 | |
A | ASN180 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
B | ASP90 | |
B | ASN180 | |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
A | ASP90 | |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2bmi |
Chain | Residue | Details |
B | ASP90 | |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 16 |
Chain | Residue | Details |
A | HIS86 | metal ligand |
A | HIS88 | metal ligand |
A | ASP90 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | HIS149 | metal ligand |
A | ASN180 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 16 |
Chain | Residue | Details |
B | HIS86 | metal ligand |
B | HIS88 | metal ligand |
B | ASP90 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | HIS149 | metal ligand |
B | ASN180 | electrostatic stabiliser, hydrogen bond donor |