2QUY
Truncated mutant ASN175ALA of penicillin v acylase from bacillus sphaericus
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008953 | molecular_function | penicillin amidase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046677 | biological_process | response to antibiotic |
B | 0008953 | molecular_function | penicillin amidase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0046677 | biological_process | response to antibiotic |
C | 0008953 | molecular_function | penicillin amidase activity |
C | 0016787 | molecular_function | hydrolase activity |
C | 0046677 | biological_process | response to antibiotic |
D | 0008953 | molecular_function | penicillin amidase activity |
D | 0016787 | molecular_function | hydrolase activity |
D | 0046677 | biological_process | response to antibiotic |
E | 0008953 | molecular_function | penicillin amidase activity |
E | 0016787 | molecular_function | hydrolase activity |
E | 0046677 | biological_process | response to antibiotic |
F | 0008953 | molecular_function | penicillin amidase activity |
F | 0016787 | molecular_function | hydrolase activity |
F | 0046677 | biological_process | response to antibiotic |
G | 0008953 | molecular_function | penicillin amidase activity |
G | 0016787 | molecular_function | hydrolase activity |
G | 0046677 | biological_process | response to antibiotic |
H | 0008953 | molecular_function | penicillin amidase activity |
H | 0016787 | molecular_function | hydrolase activity |
H | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 336 |
Chain | Residue |
A | ARG228 |
B | GLN212 |
B | HOH519 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL G 336 |
Chain | Residue |
G | PRO225 |
G | ARG228 |
H | GLN212 |
H | HOH513 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 336 |
Chain | Residue |
B | ARG228 |
A | GLN212 |
A | HOH520 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL C 336 |
Chain | Residue |
C | ARG228 |
C | HOH499 |
D | GLN212 |
D | HOH468 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL C 337 |
Chain | Residue |
C | GLN212 |
C | HOH444 |
D | ARG228 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL E 336 |
Chain | Residue |
E | PRO225 |
E | ARG228 |
F | GLN212 |
F | HOH429 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL E 337 |
Chain | Residue |
E | GLN212 |
E | HOH520 |
F | PRO225 |
F | ARG228 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL H 336 |
Chain | Residue |
G | GLN212 |
G | HOH477 |
H | PRO225 |
H | ARG228 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:10331865, ECO:0000305|PubMed:16508111 |
Chain | Residue | Details |
A | CYS1 | |
B | CYS1 | |
C | CYS1 | |
D | CYS1 | |
E | CYS1 | |
F | CYS1 | |
G | CYS1 | |
H | CYS1 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 241 |
Chain | Residue | Details |
A | CYS1 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
A | TYR82 | electrostatic stabiliser, hydrogen bond donor |
A | ALA175 | electrostatic stabiliser, hydrogen bond donor |
A | ARG228 | activator, hydrogen bond donor, increase acidity, increase basicity, repulsive charge-charge interaction |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 241 |
Chain | Residue | Details |
B | CYS1 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
B | TYR82 | electrostatic stabiliser, hydrogen bond donor |
B | ALA175 | electrostatic stabiliser, hydrogen bond donor |
B | ARG228 | activator, hydrogen bond donor, increase acidity, increase basicity, repulsive charge-charge interaction |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 241 |
Chain | Residue | Details |
C | CYS1 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
C | TYR82 | electrostatic stabiliser, hydrogen bond donor |
C | ALA175 | electrostatic stabiliser, hydrogen bond donor |
C | ARG228 | activator, hydrogen bond donor, increase acidity, increase basicity, repulsive charge-charge interaction |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 241 |
Chain | Residue | Details |
D | CYS1 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
D | TYR82 | electrostatic stabiliser, hydrogen bond donor |
D | ALA175 | electrostatic stabiliser, hydrogen bond donor |
D | ARG228 | activator, hydrogen bond donor, increase acidity, increase basicity, repulsive charge-charge interaction |
site_id | MCSA5 |
Number of Residues | 4 |
Details | M-CSA 241 |
Chain | Residue | Details |
E | CYS1 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
E | TYR82 | electrostatic stabiliser, hydrogen bond donor |
E | ALA175 | electrostatic stabiliser, hydrogen bond donor |
E | ARG228 | activator, hydrogen bond donor, increase acidity, increase basicity, repulsive charge-charge interaction |
site_id | MCSA6 |
Number of Residues | 4 |
Details | M-CSA 241 |
Chain | Residue | Details |
F | CYS1 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
F | TYR82 | electrostatic stabiliser, hydrogen bond donor |
F | ALA175 | electrostatic stabiliser, hydrogen bond donor |
F | ARG228 | activator, hydrogen bond donor, increase acidity, increase basicity, repulsive charge-charge interaction |
site_id | MCSA7 |
Number of Residues | 4 |
Details | M-CSA 241 |
Chain | Residue | Details |
G | CYS1 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
G | TYR82 | electrostatic stabiliser, hydrogen bond donor |
G | ALA175 | electrostatic stabiliser, hydrogen bond donor |
G | ARG228 | activator, hydrogen bond donor, increase acidity, increase basicity, repulsive charge-charge interaction |
site_id | MCSA8 |
Number of Residues | 4 |
Details | M-CSA 241 |
Chain | Residue | Details |
H | CYS1 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
H | TYR82 | electrostatic stabiliser, hydrogen bond donor |
H | ALA175 | electrostatic stabiliser, hydrogen bond donor |
H | ARG228 | activator, hydrogen bond donor, increase acidity, increase basicity, repulsive charge-charge interaction |