Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2HDR

AmpC beta-lactamase in complex with 4-Amino-3-hydroxybenzoic acid

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	5
Details	BINDING SITE FOR RESIDUE PO4 A 401

Chain	Residue
A	SER64
A	TYR150
A	THR316
A	ALA318
A	HOH536

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 4A3 A 501

Chain	Residue
A	HOH522
A	HOH544
A	VAL191
A	GLU196
A	TYR199
A	HIS210

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 4A3 B 502

Chain	Residue
B	VAL191
B	GLU196
B	TYR199
B	HIS210
B	HOH525
B	HOH567

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 4A3 A 503

Chain	Residue
A	GLN120
A	ASN152
A	SER212
A	TYR221
A	THR319
A	GLY320
A	HOH557
A	HOH581

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE 4A3 B 504

Chain	Residue
B	PRO140
B	TRP142
B	ALA143
B	HOH520

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 4A3 B 505

Chain	Residue
B	GLN120
B	ASN152
B	VAL211
B	SER212
B	TYR221
B	GLY320
B	HOH573
B	HOH600

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 4A3 A 506

Chain	Residue
A	LYS239
A	PRO240
A	LEU241
A	ARG309
B	LYS246
B	THR247
B	GLN250

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 4A3 B 507

Chain	Residue
A	THR302
B	TYR259
B	TRP260
B	ILE301
B	THR302
B	PRO303
B	PRO304
B	HOH571

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE 4A3 A 508

Chain	Residue
A	ALA141
A	TRP142
A	ALA143
A	HOH538

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 4A3 A 509

Chain	Residue
A	PRO277
A	PRO277
A	VAL278
A	PRO280
A	TRP354
A	ASN358
A	4A3511

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE 4A3 A 510

Chain	Residue
A	ILE48
A	GLY206
A	HOH653

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE 4A3 A 511

Chain	Residue
A	PRO277
A	VAL278
A	ASN279
A	4A3509

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 4A3 B 512

Chain	Residue
A	TRP93
A	GLU95
A	SER128
A	SER129
A	LEU132
B	ASN279
B	ASP281
B	ASN285

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 4A3 A 513

Chain	Residue
A	VAL125
A	LYS126
A	PRO213
A	GLY214
A	ALA215
A	HOH563

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 4A3 B 514

Chain	Residue
A	GLY167
A	LEU168
A	SER169
A	GLN172
B	TRP354
B	GLN355
B	ASN358

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 4A3 B 515

Chain	Residue
B	THR97
B	LYS99
B	ASN102
B	TRP188
B	ASN190
B	PRO192

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)