4KG5

Crystal Structure of AmpC beta-lactamase N152G Mutant in Complex with Cefotaxime

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	2
Details	BINDING SITE FOR RESIDUE PO4 B 401

Chain	Residue
B	HIS186
B	LYS290

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site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PCZ B 402

Chain	Residue
B	GLY320
B	ASN346
B	HOH526
B	HOH544
B	HOH546
B	HOH578
B	SER64
B	VAL211
B	TYR221
B	ASN289
B	GLY317
B	ALA318
B	THR319

---

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

Chain	Residue
A	HIS186
A	LYS290
A	PO4402
C	SER129

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 A 402

Chain	Residue
A	HIS186
A	GLU195
A	LYS197
A	ASN198
A	PO4401
A	HOH614

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 A 403

Chain	Residue
A	SER129
A	ARG133
C	HIS186

---

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PCZ A 404

Chain	Residue
A	SER64
A	VAL211
A	TYR221
A	ASN289
A	LEU293
A	GLY317
A	ALA318
A	THR319
A	GLY320
A	ASN346
A	HOH515

---

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PCZ C 401

Chain	Residue
C	SER64
C	LEU119
C	VAL211
C	TYR221
C	ASN289
C	GLY317
C	ALA318
C	GLY320
C	HOH560
C	HOH578
C	HOH619

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 D 401

Chain	Residue
B	ARG133
C	LYS290
D	HIS186
D	GLU195

---

site_id	AC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PCZ D 402

Chain	Residue
D	SER64
D	LEU119
D	GLN120
D	VAL211
D	TYR221
D	ASN289
D	GLY317
D	ALA318
D	THR319
D	GLY320
D	ASN343
D	ASN346
D	HOH507
D	HOH542
D	HOH584

---

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
B	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
B	SER64
A	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
B	SER64
C	TYR150
C	GLY152
C	ALA318
D	SER64
D	TYR150
D	GLY152
D	ALA318
B	TYR150
B	GLY152
B	ALA318
A	SER64
A	TYR150
A	GLY152
A	ALA318
C	SER64

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