4DXB
2.29A structure of the engineered MBP TEM-1 fusion protein RG13 in complex with zinc, P1 space group
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008643 | biological_process | carbohydrate transport |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0015144 | molecular_function | carbohydrate transmembrane transporter activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| A | 0055085 | biological_process | transmembrane transport |
| B | 0008643 | biological_process | carbohydrate transport |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0015144 | molecular_function | carbohydrate transmembrane transporter activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| B | 0055085 | biological_process | transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 701 |
| Chain | Residue |
| A | ASP164 |
| A | HIS468 |
| A | HOH861 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 702 |
| Chain | Residue |
| A | TYR17 |
| A | HIS39 |
| A | HIS509 |
| A | HIS514 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 701 |
| Chain | Residue |
| B | HOH803 |
| B | ASP164 |
| B | HIS468 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 702 |
| Chain | Residue |
| B | TYR17 |
| B | HIS39 |
| B | HIS509 |
| B | HIS514 |
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 | PHE422-LEU437 |
| site_id | PS01037 |
| Number of Residues | 18 |
| Details | SBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN |
| Chain | Residue | Details |
| A | PRO107-ASN124 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Acyl-ester intermediate |
| Chain | Residue | Details |
| A | SER426 | |
| B | SER426 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | GLU524 | |
| B | GLU524 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASN590 | |
| B | ASN590 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 2 |
| Chain | Residue | Details |
| A | SER426 | electrostatic stabiliser |
| A | LYS429 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | SER486 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU522 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASN590 | electrostatic stabiliser |
| A | LYS593 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 2 |
| Chain | Residue | Details |
| B | SER426 | electrostatic stabiliser |
| B | LYS429 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | SER486 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU522 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASN590 | electrostatic stabiliser |
| B | LYS593 | electrostatic stabiliser, hydrogen bond donor |
