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	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10331865","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16508111","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

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

---