Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3GSG

AmpC beta-lactamase in complex with Fragment-based 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	6
Details	BINDING SITE FOR RESIDUE PO4 A 1

Chain	Residue
A	TRP93
A	LEU157
A	LEU161
A	LYS164
A	HOH662
A	HOH811

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 2

Chain	Residue
A	HOH388
A	HOH447
A	HOH471
A	HOH596
A	HOH793
A	ALA141
A	TRP142
A	ALA143

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 362

Chain	Residue
A	GLY81
A	GLU82
A	TYR92
A	PRO165
A	HOH511

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 A 363

Chain	Residue
A	LYS84
A	LYS91
A	HOH612

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS A 364

Chain	Residue
A	ALA307
A	ARG309
B	ALA79

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DMS A 365

Chain	Residue
A	ASN285
A	GLY286
A	SER287
A	LYS290
A	ILE291
A	ASN346
A	PRO347

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GF1 A 366

Chain	Residue
A	SER64
A	TYR150
A	ASN152
A	TYR221
A	GLY317
A	ALA318
A	HOH449
A	HOH611

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GF1 A 367

Chain	Residue
A	SER129
A	ARG133
A	HIS186
A	HOH704
A	HOH737
A	HOH804
B	LYS290

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMS B 1

Chain	Residue
A	PHE41
A	THR42
B	GLY116
B	TRP142
B	LEU149

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS B 362

Chain	Residue
B	TRP93
B	LEU157
B	LYS164

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DMS B 363

Chain	Residue
B	TYR150
B	ASN289
B	ALA292
B	LYS315
B	THR316
B	ASN346
B	GF1365
B	HOH534

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 3

Chain	Residue
A	HOH456
B	ASP351
B	TRP354
B	GLN355

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMS B 364

Chain	Residue
A	GLY263
A	PRO297
B	TYR45
B	LYS51
B	HOH716

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GF1 B 365

Chain	Residue
B	SER64
B	GLN120
B	ASN152
B	TYR221
B	ALA318
B	DMS363
B	HOH392
B	HOH802

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMS B 366

Chain	Residue
B	SER127
B	SER128

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	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

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1xx2

Chain	Residue	Details
A	GLU272
A	SER64
A	LYS315
A	TYR150
A	LYS67

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1xx2

Chain	Residue	Details
B	GLU272
B	SER64
B	LYS315
B	TYR150
B	LYS67

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)