6TPM

Crystal structure of AmpC from E.coli with Relebactam (MK-7655)

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue PEG A 601

Chain	Residue
A	TRP93
A	LEU131

---

site_id	AC2
Number of Residues	15
Details	binding site for residue MK7 A 602

Chain	Residue
A	THR316
A	GLY317
A	ALA318
A	ASN346
A	SO4606
A	HOH713
A	HOH731
A	HOH810
A	SER64
A	GLN120
A	TYR150
A	ASN152
A	TYR221
A	ASN289
A	LYS315

---

site_id	AC3
Number of Residues	6
Details	binding site for residue ZN A 603

Chain	Residue
A	HIS13
A	HIS13
A	HIS13
A	CL608
A	CL608
A	CL608

---

site_id	AC4
Number of Residues	5
Details	binding site for residue ZN A 604

Chain	Residue
A	HIS186
A	HOH772
A	HOH797
A	HOH853
A	HOH936

---

site_id	AC5
Number of Residues	10
Details	binding site for residue MES A 605

Chain	Residue
A	GLN22
A	GLN23
A	LYS24
A	TYR40
A	PHE41
A	THR42
A	GLN56
A	SO4607
A	HOH806
A	HOH890

---

site_id	AC6
Number of Residues	5
Details	binding site for residue SO4 A 606

Chain	Residue
A	VAL211
A	SER212
A	THR319
A	GLY320
A	MK7602

---

site_id	AC7
Number of Residues	3
Details	binding site for residue SO4 A 607

Chain	Residue
A	GLN56
A	MES605
A	HOH732

---

site_id	AC8
Number of Residues	6
Details	binding site for residue CL A 608

Chain	Residue
A	HIS13
A	HIS13
A	HIS13
A	ZN603
A	ZN603
A	ZN603

---

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	1
Details	Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10102","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11478888","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12005439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16506777","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35486701","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6795623","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9819201","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2000","firstPage":"10504","lastPage":"10512","volume":"122","journal":"J. Am. Chem. Soc.","title":"Crystal Structures of Substrate and Inhibitor Complexes with AmpC Beta-Lactamase: Possible Implications for Substrate-Assisted Catalysis.","authors":["Patera A.","Blaszczak L.C.","Shoichet B.K."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/ja001676x"}]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16506777","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2000","firstPage":"10504","lastPage":"10512","volume":"122","journal":"J. Am. Chem. Soc.","title":"Crystal Structures of Substrate and Inhibitor Complexes with AmpC Beta-Lactamase: Possible Implications for Substrate-Assisted Catalysis.","authors":["Patera A.","Blaszczak L.C.","Shoichet B.K."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/ja001676x"}]}},{"source":"PDB","id":"1FCN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FFY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12005439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12323371","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LL9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16506777","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2FFY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12005439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12323371","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16506777","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2000","firstPage":"10504","lastPage":"10512","volume":"122","journal":"J. Am. Chem. Soc.","title":"Crystal Structures of Substrate and Inhibitor Complexes with AmpC Beta-Lactamase: Possible Implications for Substrate-Assisted Catalysis.","authors":["Patera A.","Blaszczak L.C.","Shoichet B.K."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/ja001676x"}]}},{"source":"PDB","id":"1FCN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LL9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FFY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12005439","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KVM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---