4KG6

Crystal Structure of AmpC beta-lactamase N152G Mutant from E. coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008800	molecular_function	beta-lactamase activity
A	0016787	molecular_function	hydrolase activity
A	0017001	biological_process	antibiotic catabolic process
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042597	cellular_component	periplasmic space
A	0046677	biological_process	response to antibiotic
B	0008800	molecular_function	beta-lactamase activity
B	0016787	molecular_function	hydrolase activity
B	0017001	biological_process	antibiotic catabolic process
B	0030288	cellular_component	outer membrane-bounded periplasmic space
B	0042597	cellular_component	periplasmic space
B	0046677	biological_process	response to antibiotic
C	0008800	molecular_function	beta-lactamase activity
C	0016787	molecular_function	hydrolase activity
C	0017001	biological_process	antibiotic catabolic process
C	0030288	cellular_component	outer membrane-bounded periplasmic space
C	0042597	cellular_component	periplasmic space
C	0046677	biological_process	response to antibiotic
D	0008800	molecular_function	beta-lactamase activity
D	0016787	molecular_function	hydrolase activity
D	0017001	biological_process	antibiotic catabolic process
D	0030288	cellular_component	outer membrane-bounded periplasmic space
D	0042597	cellular_component	periplasmic space
D	0046677	biological_process	response to antibiotic

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 401

Chain	Residue
A	LYS84
A	LYS91
A	HOH734
A	HOH837

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 A 402

Chain	Residue
A	HOH527
A	HOH567
A	HOH761
A	HOH831
A	SER64
A	TYR150
A	THR316
A	GLY317
A	ALA318

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 401

Chain	Residue
B	HIS186
B	LYS290
B	HOH861
D	SER129

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 B 402

Chain	Residue
B	SER64
B	TYR150
B	LYS315
B	THR316
B	GLY317
B	ALA318
B	HOH594
B	HOH611
B	HOH892

---

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 C 401

Chain	Residue
A	ARG133
C	HIS186
C	GLU195
C	LYS197
C	ASN198
C	HOH663
C	HOH742
C	HOH789
D	LYS290

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 C 402

Chain	Residue
B	SER129
B	ARG133
D	GLN57
D	HIS186

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 C 403

Chain	Residue
C	ARG80
C	HOH533
C	HOH566
C	HOH684

---

Functional Information from PROSITE/UniProt

site_id	PS00336
Number of Residues	8
Details	BETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK

Chain	Residue	Details
A	PHE60-LYS67

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102, ECO:0000269|PubMed:11478888, ECO:0000269|PubMed:16506777, ECO:0000269|PubMed:6795623, ECO:0000269|PubMed:9819201

Chain	Residue	Details
A	SER64
B	SER64
C	SER64
D	SER64

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0007744|PDB:2FFY

Chain	Residue	Details
C	TYR150
C	GLY152
C	ALA318
D	SER64
D	TYR150
D	GLY152
D	ALA318
B	SER64
B	TYR150
B	GLY152
B	ALA318
C	SER64
A	SER64
A	TYR150
A	GLY152
A	ALA318

---