4PEL

S1C mutant of Penicillin G acylase from Kluyvera citrophila

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016787	molecular_function	hydrolase activity
A	0016811	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A	0017000	biological_process	antibiotic biosynthetic process
B	0016787	molecular_function	hydrolase activity
B	0016811	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
B	0017000	biological_process	antibiotic biosynthetic process
C	0016787	molecular_function	hydrolase activity
C	0016811	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
C	0017000	biological_process	antibiotic biosynthetic process
D	0016787	molecular_function	hydrolase activity
D	0016811	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
D	0017000	biological_process	antibiotic biosynthetic process
E	0016787	molecular_function	hydrolase activity
E	0016811	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
E	0017000	biological_process	antibiotic biosynthetic process
F	0016787	molecular_function	hydrolase activity
F	0016811	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
F	0017000	biological_process	antibiotic biosynthetic process
G	0016787	molecular_function	hydrolase activity
G	0016811	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
G	0017000	biological_process	antibiotic biosynthetic process
H	0016787	molecular_function	hydrolase activity
H	0016811	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
H	0017000	biological_process	antibiotic biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue CA A 601

Chain	Residue
A	GLU152
B	ASP73
B	VAL75
B	ASP76
B	PRO205
B	ASP252

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site_id	AC2
Number of Residues	6
Details	binding site for residue CA C 601

Chain	Residue
D	ASP76
D	PRO205
D	ASP252
C	GLU152
D	ASP73
D	VAL75

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site_id	AC3
Number of Residues	6
Details	binding site for residue CA E 601

Chain	Residue
E	GLU152
F	ASP73
F	VAL75
F	ASP76
F	PRO205
F	ASP252

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site_id	AC4
Number of Residues	6
Details	binding site for residue CA G 601

Chain	Residue
G	GLU152
H	ASP73
H	VAL75
H	ASP76
H	PRO205
H	ASP252

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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