4E3I

Crystal structure of AmpC beta-lactamase in complex with a designed 3-carboxyl benzyl sulfonamide boronic acid inhibitor

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 0N3 A 401

Chain	Residue
A	SER64
A	THR319
A	GLY320
A	PO4404
A	HOH504
A	HOH556
A	HOH826
A	GLN120
A	TYR150
A	ASN152
A	VAL211
A	SER212
A	TYR221
A	GLY317
A	ALA318

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 A 402

Chain	Residue
A	TYR45
A	ILE48
A	HOH716

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 403

Chain	Residue
A	PRO140
A	ALA141
A	TRP142
A	ALA143
A	HOH715

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 404

Chain	Residue
A	ASN289
A	LEU293
A	0N3401
A	HOH638

---

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 0N3 B 401

Chain	Residue
B	SER64
B	GLN120
B	TYR150
B	ASN152
B	VAL211
B	SER212
B	TYR221
B	GLY317
B	ALA318
B	THR319
B	GLY320
B	PO4402
B	HOH547
B	HOH561
B	HOH716

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 B 402

Chain	Residue
B	TYR150
B	ASN289
B	LEU293
B	0N3401
B	HOH642

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 B 403

Chain	Residue
A	ARG133
A	HIS186
A	HOH615
A	HOH659
B	LYS290

---

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	2
Details	ACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102, ECO:0000269|PubMed:11478888, ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:16506777, ECO:0000269|PubMed:6795623, ECO:0000269|PubMed:9819201, ECO:0000269|DOI:10.1021/ja001676x

Chain	Residue	Details
A	SER64
B	SER64

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0000269|DOI:10.1021/ja001676x, ECO:0007744|PDB:1FCN, ECO:0007744|PDB:2FFY

Chain	Residue	Details
A	SER64
B	SER64

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:12323371, ECO:0007744|PDB:1KVM, ECO:0007744|PDB:1LL9

Chain	Residue	Details
A	GLN120
B	GLN120

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0007744|PDB:2FFY

Chain	Residue	Details
A	TYR150
B	TYR150

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:12323371, ECO:0000269|PubMed:16506777, ECO:0000269|DOI:10.1021/ja001676x, ECO:0007744|PDB:1FCN, ECO:0007744|PDB:1KVM, ECO:0007744|PDB:1LL9, ECO:0007744|PDB:2FFY

Chain	Residue	Details
A	ASN152
A	ALA318
B	ASN152
B	ALA318

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0007744|PDB:1KVM

Chain	Residue	Details
A	ASN343
B	ASN343

---