2BFZ
Bacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH4.5 using 20mM ZnSO4 in buffer. 1mM DTT was used as a reducing agent. Cys221 is oxidized.
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 GOL A 1293 |
| Chain | Residue |
| A | ASP88 |
| A | ASP89 |
| A | LYS90 |
| A | HOH2180 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 1294 |
| Chain | Residue |
| A | HOH2181 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1295 |
| Chain | Residue |
| A | HOH2184 |
| A | ASN184 |
| A | LYS186 |
| A | GLN210 |
| A | HOH2183 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1296 |
| Chain | Residue |
| A | HIS116 |
| A | HIS118 |
| A | HIS196 |
| A | CSD221 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1297 |
| Chain | Residue |
| A | GLU97 |
| A | ARG131 |
| A | ARG254 |
| A | ILE256 |
| A | LYS280 |
| A | HOH2055 |
| A | HOH2185 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1298 |
| Chain | Residue |
| A | SER225 |
| A | THR226 |
| A | SER227 |
| A | GLY264 |
| A | GLU265 |
| A | HOH2063 |
| A | HOH2186 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1299 |
| Chain | Residue |
| A | LYS147 |
| B | ARG107 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1300 |
| Chain | Residue |
| B | GLN47 |
| B | TRP53 |
| B | LYS103 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1292 |
| Chain | Residue |
| B | THR139 |
| B | LEU141 |
| B | GLN175 |
| B | THR176 |
| B | GOL1295 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 1293 |
| Chain | Residue |
| B | ALA228 |
| B | LYS229 |
| B | ASP230 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE AZI B 1294 |
| Chain | Residue |
| B | HIS196 |
| B | CSO221 |
| B | LYS224 |
| B | ASN233 |
| B | HOH2082 |
| B | HOH2175 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 1295 |
| Chain | Residue |
| B | LYS78 |
| B | GLN175 |
| B | GOL1292 |
| B | HOH2113 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 1296 |
| Chain | Residue |
| B | LEU58 |
| B | ALA66 |
| B | HOH2178 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1297 |
| Chain | Residue |
| B | HIS116 |
| B | HIS118 |
| B | HIS196 |
| B | HOH2082 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1298 |
| Chain | Residue |
| B | SER225 |
| B | THR226 |
| B | SER227 |
| B | GLY264 |
| B | GLU265 |
| B | HOH2160 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1299 |
| Chain | Residue |
| B | LYS129 |
| B | GLU168 |
| B | GLU169 |
| B | HOH2180 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1300 |
| Chain | Residue |
| B | LYS181 |
| B | LYS186 |
| B | ARG252 |
| B | HOH2181 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 1301 |
| Chain | Residue |
| B | GLU97 |
| B | ARG107 |
| B | ARG131 |
Functional Information from PROSITE/UniProt
| site_id | PS00743 |
| Number of Residues | 20 |
| Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IiTHaHADciGGiktlker.G |
| Chain | Residue | Details |
| B | ILE113-GLY133 | |
| A | ILE113-GLY133 |
| site_id | PS00744 |
| Number of Residues | 13 |
| Details | BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PqynILvGgCLVK |
| Chain | Residue | Details |
| B | PRO209-LYS224 | |
| A | PRO209-LYS224 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20677753","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24059435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7588620","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9761898","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20677753","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24059435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9761898","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| A | ASP120 | |
| A | ASN233 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| B | ASP120 | |
| B | ASN233 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| A | ASP120 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2bmi |
| Chain | Residue | Details |
| B | ASP120 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 16 |
| Chain | Residue | Details |
| B | HIS116 | metal ligand |
| B | HIS118 | metal ligand |
| B | ASP120 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | HIS196 | metal ligand |
| B | ALA237 | electrostatic stabiliser, hydrogen bond donor |
