1JTD
Crystal structure of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase 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 | 0005737 | cellular_component | cytoplasm |
| B | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| B | 0016567 | biological_process | protein ubiquitination |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0061630 | molecular_function | ubiquitin protein ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 501 |
| Chain | Residue |
| A | GLU37 |
| A | HOH503 |
| A | HOH509 |
| B | GLY221 |
| B | ASP223 |
| B | ASP237 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 502 |
| Chain | Residue |
| B | HOH534 |
| B | HOH586 |
| B | HOH683 |
| B | ASP187 |
| B | GLY188 |
| B | HOH506 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 503 |
| Chain | Residue |
| B | GLY104 |
| B | ASP106 |
| B | ASP120 |
| B | HOH703 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 504 |
| Chain | Residue |
| B | GLY166 |
| B | HOH608 |
| B | HOH671 |
| B | HOH697 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 505 |
| Chain | Residue |
| B | THR184 |
| B | HOH590 |
| B | HOH591 |
| B | HOH607 |
| B | HOH700 |
Functional Information from PROSITE/UniProt
| site_id | PS00146 |
| Number of Residues | 16 |
| Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FpMMSTfKvllCGAVL |
| Chain | Residue | Details |
| A | PHE66-LEU81 |
| site_id | PS00626 |
| Number of Residues | 11 |
| Details | RCC1_2 Regulator of chromosome condensation (RCC1) signature 2. IAGGyFHGLAL |
| Chain | Residue | Details |
| B | ILE69-LEU79 | |
| B | ILE108-LEU118 | |
| B | VAL225-LEU235 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Acyl-ester intermediate |
| Chain | Residue | Details |
| A | SER70 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | GLU168 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS234 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1btl |
| Chain | Residue | Details |
| A | GLU166 | |
| A | LYS73 | |
| A | SER130 | |
| A | SER70 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 2 |
| Chain | Residue | Details |
| A | SER70 | electrostatic stabiliser |
| A | LYS73 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | SER130 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU166 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | LYS234 | electrostatic stabiliser |
| A | ALA237 | electrostatic stabiliser, hydrogen bond donor |
