Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6R79

Structure of IMP-13 metallo-beta-lactamase in apo form (loop open)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008270	molecular_function	zinc ion binding
A	0008800	molecular_function	beta-lactamase activity
A	0016787	molecular_function	hydrolase activity
A	0017001	biological_process	antibiotic catabolic process
A	0042597	cellular_component	periplasmic space
A	0046677	biological_process	response to antibiotic
A	0046872	molecular_function	metal ion binding
B	0008270	molecular_function	zinc ion binding
B	0008800	molecular_function	beta-lactamase activity
B	0016787	molecular_function	hydrolase activity
B	0017001	biological_process	antibiotic catabolic process
B	0042597	cellular_component	periplasmic space
B	0046677	biological_process	response to antibiotic
B	0046872	molecular_function	metal ion binding
C	0008270	molecular_function	zinc ion binding
C	0008800	molecular_function	beta-lactamase activity
C	0016787	molecular_function	hydrolase activity
C	0017001	biological_process	antibiotic catabolic process
C	0042597	cellular_component	periplasmic space
C	0046677	biological_process	response to antibiotic
C	0046872	molecular_function	metal ion binding
D	0008270	molecular_function	zinc ion binding
D	0008800	molecular_function	beta-lactamase activity
D	0016787	molecular_function	hydrolase activity
D	0017001	biological_process	antibiotic catabolic process
D	0042597	cellular_component	periplasmic space
D	0046677	biological_process	response to antibiotic
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue GOL A 301

Chain	Residue
A	SER99
A	GLU100
A	LEU101
A	SER119
A	TYR134
A	LEU144
A	HOH455
A	HOH524

site_id	AC2
Number of Residues	2
Details	binding site for residue BME A 302

Chain	Residue
A	PRO135
A	TYR134

site_id	AC3
Number of Residues	6
Details	binding site for residue GOL A 303

Chain	Residue
A	LEU39
A	VAL40
A	GLU150
A	SER151
A	HOH483
A	HOH512

site_id	AC4
Number of Residues	4
Details	binding site for residue GLY A 304

Chain	Residue
A	GLU10
A	HIS34
A	LYS200
A	HOH440

site_id	AC5
Number of Residues	5
Details	binding site for residue GLY A 305

Chain	Residue
A	GLU120
A	VAL121
A	SER122
A	HOH469
A	HOH516

site_id	AC6
Number of Residues	5
Details	binding site for residue BME A 306

Chain	Residue
A	LYS58
A	GLY309
A	HOH450
D	HOH1218
D	HOH1250

site_id	AC7
Number of Residues	7
Details	binding site for residue GLY A 307

Chain	Residue
A	GLN141
A	ASP170
A	ALA171
A	HOH421
A	HOH447
A	HOH490
A	HOH547

site_id	AC8
Number of Residues	6
Details	binding site for residue GLY A 308

Chain	Residue
A	VAL25
A	ASN26
A	TRP28
A	GLY29
A	GLY311
D	GLY1104

site_id	AC9
Number of Residues	5
Details	binding site for residue GLY A 309

Chain	Residue
A	TRP62
A	ARG66
A	BME306
A	HOH416
A	HOH487

site_id	AD1
Number of Residues	7
Details	binding site for residue BME A 310

Chain	Residue
A	LYS108
A	HOH487
A	HOH532
A	HOH591
D	LYS107
D	GLY110
D	HOH1299

site_id	AD2
Number of Residues	8
Details	binding site for residue GLY A 311

Chain	Residue
A	VAL25
A	ASN26
A	TRP28
A	GLY308
A	HOH518
A	HOH539
D	VAL31
D	HIS197

site_id	AD3
Number of Residues	5
Details	binding site for residue ZN A 312

Chain	Residue
A	HIS77
A	HIS79
A	HIS139
A	ZN313
A	HOH562

site_id	AD4
Number of Residues	6
Details	binding site for residue ZN A 313

Chain	Residue
A	ASP81
A	CYS158
A	HIS197
A	ZN312
A	HOH553
A	HOH562

site_id	AD5
Number of Residues	9
Details	binding site for residue GOL B 301

Chain	Residue
B	SER99
B	GLU100
B	LEU101
B	SER119
B	TYR134
B	LEU144
B	HOH437
B	HOH471
B	HOH516

site_id	AD6
Number of Residues	4
Details	binding site for residue BME B 302

Chain	Residue
B	PHE133
B	TYR134
B	PRO135
B	HOH415

site_id	AD7
Number of Residues	5
Details	binding site for residue ZN B 303

Chain	Residue
B	HIS77
B	HIS79
B	HIS139
B	ZN304
C	HOH493

site_id	AD8
Number of Residues	6
Details	binding site for residue ZN B 304

Chain	Residue
B	ASP81
B	CYS158
B	HIS197
B	ZN303
C	ASN26
C	HOH493

site_id	AD9
Number of Residues	7
Details	binding site for residue PO4 B 305

Chain	Residue
B	LEU39
B	VAL40
B	GLU150
B	HOH416
B	HOH417
B	HOH483
B	VAL38

site_id	AE1
Number of Residues	9
Details	binding site for residue GOL C 301

Chain	Residue
C	SER99
C	GLU100
C	LEU101
C	SER119
C	TYR134
C	LEU144
C	HOH442
C	HOH467
C	HOH500

site_id	AE2
Number of Residues	5
Details	binding site for residue GLY C 302

Chain	Residue
C	LEU39
C	SER151
C	HOH430
C	HOH443
C	HOH537

site_id	AE3
Number of Residues	2
Details	binding site for residue GLY C 303

Chain	Residue
C	LYS200
C	HOH404

site_id	AE4
Number of Residues	4
Details	binding site for residue GLY C 304

Chain	Residue
C	LEU7
C	ILE9
C	TRP62
C	HOH520

site_id	AE5
Number of Residues	6
Details	binding site for residue GLY C 305

Chain	Residue
B	LYS107
C	TRP210
C	GLU211
C	LEU214
C	HOH401
C	HOH471

site_id	AE6
Number of Residues	10
Details	binding site for residue BME C 306

Chain	Residue
B	HOH442
C	HIS79
C	ASP81
C	HIS139
C	ASN167
C	ZN307
C	ZN308
C	HOH503
C	HOH507
C	HOH559

site_id	AE7
Number of Residues	6
Details	binding site for residue ZN C 307

Chain	Residue
C	HIS77
C	HIS79
C	HIS139
C	BME306
C	ZN308
C	HOH507

site_id	AE8
Number of Residues	6
Details	binding site for residue ZN C 308

Chain	Residue
C	ASP81
C	CYS158
C	HIS197
C	BME306
C	ZN307
C	HOH507

site_id	AE9
Number of Residues	8
Details	binding site for residue GLY D 1101

Chain	Residue
A	VAL31
A	HIS197
D	VAL25
D	ASN26
D	HOH1239
D	HOH1249
D	HOH1276
D	HOH1293

site_id	AF1
Number of Residues	8
Details	binding site for residue GOL D 1102

Chain	Residue
D	GLU100
D	LEU101
D	SER119
D	TYR134
D	LEU144
D	HOH1259
D	HOH1280
D	HOH1314

site_id	AF2
Number of Residues	8
Details	binding site for residue GOL D 1103

Chain	Residue
D	GLU14
D	LEU39
D	LEU148
D	GLU150
D	SER151
D	HOH1215
D	HOH1282
D	HOH1351

site_id	AF3
Number of Residues	3
Details	binding site for residue GLY D 1104

Chain	Residue
A	VAL30
A	GLY308
D	VAL30

site_id	AF4
Number of Residues	3
Details	binding site for residue BME D 1105

Chain	Residue
D	TYR134
D	HOH1234
D	HOH1424

site_id	AF5
Number of Residues	2
Details	binding site for residue GLY D 1106

Chain	Residue
D	HOH1279
D	HOH1288

site_id	AF6
Number of Residues	5
Details	binding site for residue ZN D 1107

Chain	Residue
D	HIS77
D	HIS79
D	HIS139
D	ZN1108
D	HOH1341

site_id	AF7
Number of Residues	6
Details	binding site for residue ZN D 1108

Chain	Residue
A	HOH518
D	ASP81
D	CYS158
D	HIS197
D	ZN1107
D	HOH1341

Functional Information from PROSITE/UniProt

site_id	PS00743
Number of Residues	20
Details	BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IsSHfHSDstGGiewlnsq.S

Chain	Residue	Details
A	ILE74-SER93

site_id	PS00744
Number of Residues	13
Details	BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PeskILfGgCFIK

Chain	Residue	Details
A	PRO149-LYS161

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32205343","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2020","submissionDatabase":"PDB data bank","title":"Structure of IMP-13 metallo-beta-lactamase complexed with citrate anion.","authors":["Zak K.M.","Zhou R.X.","Softley C.A.","Bostock M.J.","Sattler M.","Popowicz G.M."]}},{"source":"PDB","id":"6R73","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6R79","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6RZR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6RZS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6S0H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6YI4","evidenceCode":"ECO:0007744"}]}