2NZE
Structure of beta-lactamase II from Bacillus cereus. R121H, C221S double mutant. Space group P3121.
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 |
| Chain | Residue |
| A | ASN162 |
| 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
| 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 | 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 |
