6WHF

class C beta-lactamase from Escherichia coli in complex with cephalothin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008800	molecular_function	beta-lactamase activity
A	0017001	biological_process	antibiotic catabolic process
A	0030288	cellular_component	outer membrane-bounded periplasmic space
B	0008800	molecular_function	beta-lactamase activity
B	0017001	biological_process	antibiotic catabolic process
B	0030288	cellular_component	outer membrane-bounded periplasmic space

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue EDO A 501

Chain	Residue
A	GLU299
A	SER314
A	HIS341
A	LYS342
A	THR343
A	HOH629
A	HOH632
A	HOH642

---

site_id	AC2
Number of Residues	3
Details	binding site for residue EDO A 502

Chain	Residue
A	EDO503
A	HOH620
A	THR69

---

site_id	AC3
Number of Residues	3
Details	binding site for residue EDO A 503

Chain	Residue
A	PHE68
A	THR69
A	EDO502

---

site_id	AC4
Number of Residues	6
Details	binding site for residue EDO A 504

Chain	Residue
A	LYS153
A	PRO240
A	GLY241
A	ALA242
A	HOH686
A	HOH715

---

site_id	AC5
Number of Residues	4
Details	binding site for residue EDO A 505

Chain	Residue
A	ARG107
A	THR203
A	GLU272
A	HOH639

---

site_id	AC6
Number of Residues	12
Details	binding site for residue 9EP A 506

Chain	Residue
A	SER91
A	GLN147
A	ASN179
A	TYR248
A	ASN316
A	GLY344
A	ALA345
A	THR346
A	GLY347
A	ASN370
A	HOH704
A	HOH723

---

site_id	AC7
Number of Residues	1
Details	binding site for residue EDO B 501

Chain	Residue
B	HIS237

---

site_id	AC8
Number of Residues	7
Details	binding site for residue EDO B 502

Chain	Residue
B	GLU299
B	HIS341
B	LYS342
B	THR343
B	HOH626
B	HOH641
B	HOH644

---

site_id	AC9
Number of Residues	4
Details	binding site for residue EDO B 503

Chain	Residue
B	ILE311
B	PRO374
B	ALA375
B	HOH744

---

site_id	AD1
Number of Residues	7
Details	binding site for residue EDO B 504

Chain	Residue
B	GLY108
B	GLU109
B	ILE110
B	LYS111
B	ASP114
B	LYS118
B	TYR119

---

site_id	AD2
Number of Residues	10
Details	binding site for residue 9EP B 505

Chain	Residue
B	SER91
B	GLN147
B	ASN179
B	TYR248
B	ASN316
B	GLY344
B	ALA345
B	GLY347
B	ASN370
B	HOH730

---

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	PHE87-LYS94

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
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	2
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	2
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	2
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	4
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	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12005439","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KVM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---