6YEO

Crystal structure of AmpC from E. coli with cyclic boronate 2

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	13
Details	binding site for residue OK3 A 401

Chain	Residue
A	SER64
A	GLY320
A	ASN346
A	HOH518
A	HOH536
A	TYR150
A	ASN152
A	TYR221
A	ASN289
A	LYS315
A	THR316
A	GLY317
A	ALA318

---

site_id	AC2
Number of Residues	5
Details	binding site for residue MPD A 402

Chain	Residue
A	ARG232
A	SER236
A	ILE243
A	HOH581
A	HOH620

---

site_id	AC3
Number of Residues	12
Details	binding site for residue EPE A 403

Chain	Residue
A	ILE78
A	LYS84
A	LEU85
A	SER86
A	LEU254
A	SER257
A	PRO304
A	HOH511
A	HOH671
C	PRO303
C	PRO306
C	HOH526

---

site_id	AC4
Number of Residues	3
Details	binding site for residue NA A 404

Chain	Residue
A	HIS108
A	HOH651
C	HOH633

---

site_id	AC5
Number of Residues	2
Details	binding site for residue CL A 405

Chain	Residue
A	THR55
A	GLN56

---

site_id	AC6
Number of Residues	3
Details	binding site for residue MPD B 402

Chain	Residue
B	ASP242
D	ALA79
D	ARG80

---

site_id	AC7
Number of Residues	3
Details	binding site for residue GOL B 403

Chain	Residue
B	SER236
B	HOH560
B	HOH561

---

site_id	AC8
Number of Residues	3
Details	binding site for residue CL B 404

Chain	Residue
B	GLN175
B	ILE189
B	ASN190

---

site_id	AC9
Number of Residues	1
Details	binding site for residue GOL C 402

Chain	Residue
C	ASP242

---

site_id	AD1
Number of Residues	4
Details	binding site for residue GOL C 403

Chain	Residue
C	GLN52
C	LYS197
C	TYR199
C	TRP201

---

site_id	AD2
Number of Residues	3
Details	binding site for residue GOL C 404

Chain	Residue
C	LEU182
C	SER236
C	ILE243

---

site_id	AD3
Number of Residues	3
Details	binding site for residue MPD D 402

Chain	Residue
D	PRO140
D	TRP142
D	HOH501

---

site_id	AD4
Number of Residues	13
Details	binding site for residue EPE D 403

Chain	Residue
B	PRO304
B	PRO306
B	HOH592
D	ILE78
D	LYS84
D	LEU85
D	SER86
D	LEU254
D	SER257
D	PRO304
D	HOH509
D	HOH521
D	HOH584

---

site_id	AD5
Number of Residues	18
Details	binding site for Di-peptide OK3 B 401 and SER B 64

Chain	Residue
B	LEU62
B	GLY63
B	VAL65
B	SER66
B	LYS67
B	TYR150
B	ASN152
B	ALA220
B	TYR221
B	ASN289
B	LYS315
B	THR316
B	GLY317
B	ALA318
B	THR319
B	GLY320
B	ASN346
B	HOH501

---

site_id	AD6
Number of Residues	20
Details	binding site for Di-peptide OK3 C 401 and SER C 64

Chain	Residue
C	GLY317
C	ALA318
C	THR319
C	GLY320
C	ASN346
C	HOH503
C	HOH542
C	LEU62
C	GLY63
C	VAL65
C	SER66
C	LYS67
C	TYR150
C	ASN152
C	ARG204
C	ALA220
C	TYR221
C	ASN289
C	LYS315
C	THR316

---

site_id	AD7
Number of Residues	19
Details	binding site for Di-peptide OK3 D 401 and SER D 64

Chain	Residue
D	LEU62
D	GLY63
D	VAL65
D	SER66
D	LYS67
D	TYR150
D	ASN152
D	ALA220
D	TYR221
D	ASN289
D	LYS315
D	THR316
D	GLY317
D	ALA318
D	GLY320
D	ASN346
D	HOH504
D	HOH534
D	HOH537

---

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

---

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:6795623

Chain	Residue	Details
B	SER64
C	SER64
D	SER64
A	SER64

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
B	TYR150
C	TYR150
D	TYR150
A	TYR150

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	LYS315
B	LYS315
C	LYS315
D	LYS315

---