Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3GRJ

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	8
Details	BINDING SITE FOR RESIDUE PO4 A 2

Chain	Residue
A	SER64
A	TYR150
A	ASN289
A	LYS315
A	THR316
A	GLY317
A	ALA318
A	HOH471

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 362

Chain	Residue
A	LEU131
A	LEU161
A	LYS164
A	TRP93

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PO4 A 363

Chain	Residue
A	ARG80

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE G14 A 1

Chain	Residue
A	SER129
A	ARG133
A	HIS186
A	HOH489
B	LYS290

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG A 364

Chain	Residue
A	PRO140
A	ALA141
A	ALA143
A	HOH486
A	HOH487

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE G14 A 365

Chain	Residue
A	SER166
A	GLY167
A	LEU168
A	HOH488
B	ASN358
B	ALA359
B	GLN361

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 B 1

Chain	Residue
B	SER64
B	TYR150
B	THR316
B	GLY317
B	ALA318
B	G14363
B	HOH412

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 B 3

Chain	Residue
A	ARG14
B	ARG80
B	HOH404

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 B 362

Chain	Residue
B	SER127
B	SER128

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE G14 B 363

Chain	Residue
B	PO41
B	SER64
B	GLN120
B	TYR150
B	ASN152
B	DMS368

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMS B 364

Chain	Residue
A	ASP288
A	ASN289
A	LEU293
B	TYR40
B	HOH482

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG B 365

Chain	Residue
B	PRO140
B	TRP142
B	ALA143
B	HOH466
B	HOH468

site_id	BC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PEG B 366

Chain	Residue
B	ARG148
B	TYR150
B	GLU272
B	ILE283
B	GLY286
B	SER287
B	ALA292
B	HIS314
B	HOH396
B	HOH475
B	HOH481

site_id	BC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE DMS B 367

Chain	Residue
B	GLU205

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMS B 368

Chain	Residue
B	GLN120
B	G14363

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)