2Z71

Structure of truncated mutant CYS1GLY of penicillin V acylase from bacillus sphaericus co-crystallized with penicillin V

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
C	0008953	molecular_function	penicillin amidase activity
C	0016787	molecular_function	hydrolase activity
C	0046677	biological_process	response to antibiotic

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PNV A 903

Chain	Residue
A	ASP20
A	TYR82
A	ASN175
A	PRO225
A	ARG228
A	GLU270
A	ASP274
C	GLY211
C	GLN212

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site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PNV C 904

Chain	Residue
A	GLY211
A	GLN212
C	ASP20
C	TYR82
C	ASN175
C	ARG228
C	THR268
C	ASN269
C	GLU270
C	LYS272
C	ASP274

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE:

Chain	Residue	Details
A	GLY1
C	GLY1

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 241

Chain	Residue	Details
A	GLY1	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
A	TYR82	electrostatic stabiliser, hydrogen bond donor
A	ASN175	electrostatic stabiliser, hydrogen bond donor
A	ARG228	activator, hydrogen bond donor, increase acidity, increase basicity, repulsive charge-charge interaction

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site_id	MCSA2
Number of Residues	4
Details	M-CSA 241

Chain	Residue	Details
C	GLY1	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
C	TYR82	electrostatic stabiliser, hydrogen bond donor
C	ASN175	electrostatic stabiliser, hydrogen bond donor
C	ARG228	activator, hydrogen bond donor, increase acidity, increase basicity, repulsive charge-charge interaction

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