Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5EV8

Crystal structure of the metallo-beta-lactamase IMP-1 in complex with the bisthiazolidine inhibitor D-CS319

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	5
Details	binding site for residue ZN A 301

Chain	Residue
A	HIS77
A	HIS79
A	HIS139
A	ZN302
A	3R9303

site_id	AC2
Number of Residues	5
Details	binding site for residue ZN A 302

Chain	Residue
A	3R9303
A	ASP81
A	CYS158
A	HIS197
A	ZN301

site_id	AC3
Number of Residues	10
Details	binding site for residue 3R9 A 303

Chain	Residue
A	VAL31
A	HIS79
A	ASP81
A	HIS139
A	CYS158
A	LYS161
A	ASN167
A	HIS197
A	ZN301
A	ZN302

site_id	AC4
Number of Residues	6
Details	binding site for residue 3R9 A 304

Chain	Residue
A	GLY110
A	LYS111
A	VAL112
A	HOH428
C	TRP28
C	CL307

site_id	AC5
Number of Residues	5
Details	binding site for residue ZN B 301

Chain	Residue
B	ASP81
B	CYS158
B	HIS197
B	ZN302
B	3R9303

site_id	AC6
Number of Residues	5
Details	binding site for residue ZN B 302

Chain	Residue
B	HIS77
B	HIS79
B	HIS139
B	ZN301
B	3R9303

site_id	AC7
Number of Residues	13
Details	binding site for residue 3R9 B 303

Chain	Residue
B	HIS77
B	HIS79
B	ASP81
B	HIS139
B	CYS158
B	LYS161
B	LEU165
B	GLY166
B	ASN167
B	HIS197
B	ZN301
B	ZN302
B	HOH443

site_id	AC8
Number of Residues	7
Details	binding site for residue EDO B 304

Chain	Residue
B	GLU65
B	THR83
B	GLY84
B	ILE86
B	GLU87
B	VAL112
B	HOH423

site_id	AC9
Number of Residues	5
Details	binding site for residue EDO B 305

Chain	Residue
A	ASN116
B	ASN90
B	VAL112
B	GLN113
B	HOH455

site_id	AD1
Number of Residues	6
Details	binding site for residue EDO B 306

Chain	Residue
A	TYR97
A	LEU125
B	LYS107
B	GLN113
B	HOH410
B	HOH430

site_id	AD2
Number of Residues	8
Details	binding site for residue DMS B 307

Chain	Residue
B	GLU14
B	GLY15
B	VAL16
B	VAL38
B	LEU39
B	GLU150
B	ARG151
B	HOH435

site_id	AD3
Number of Residues	5
Details	binding site for residue ZN C 301

Chain	Residue
C	HIS77
C	HIS79
C	HIS139
C	ZN302
C	3R9303

site_id	AD4
Number of Residues	4
Details	binding site for residue ZN C 302

Chain	Residue
C	CYS158
C	HIS197
C	ZN301
C	3R9303

site_id	AD5
Number of Residues	13
Details	binding site for residue 3R9 C 303

Chain	Residue
A	GLU87
C	GLU23
C	HIS77
C	HIS79
C	HIS139
C	CYS158
C	LYS161
C	LEU165
C	GLY166
C	ASN167
C	HIS197
C	ZN301
C	ZN302

site_id	AD6
Number of Residues	5
Details	binding site for residue EDO C 304

Chain	Residue
C	ASP170
C	HOH413
C	HOH458
C	LYS108
C	ASP109

site_id	AD7
Number of Residues	5
Details	binding site for residue DMS C 305

Chain	Residue
C	SER99
C	PHE118
C	GLY120
C	HOH403
C	HOH453

site_id	AD8
Number of Residues	1
Details	binding site for residue CL C 307

Chain	Residue
A	3R9304

site_id	AD9
Number of Residues	5
Details	binding site for residue ZN D 301

Chain	Residue
D	HIS77
D	HIS79
D	HIS139
D	ZN302
D	3R9303

site_id	AE1
Number of Residues	5
Details	binding site for residue ZN D 302

Chain	Residue
D	ASP81
D	CYS158
D	HIS197
D	ZN301
D	3R9303

site_id	AE2
Number of Residues	10
Details	binding site for residue 3R9 D 303

Chain	Residue
D	HIS79
D	ASP81
D	HIS139
D	CYS158
D	LYS161
D	GLY166
D	ASN167
D	HIS197
D	ZN301
D	ZN302

site_id	AE3
Number of Residues	2
Details	binding site for residue EDO D 304

Chain	Residue
C	LYS108
D	GLY27

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PRO149-LYS161

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	BINDING: BINDING => ECO:0000269\|PubMed:26482303

Chain	Residue	Details
A	HIS77
B	ASP81
B	HIS139
B	CYS158
B	LYS161
B	HIS197
C	HIS77
C	HIS79
C	ASP81
C	HIS139
C	CYS158
A	HIS79
C	LYS161
C	HIS197
D	HIS77
D	HIS79
D	ASP81
D	HIS139
D	CYS158
D	LYS161
D	HIS197
A	ASP81
A	HIS139
A	CYS158
A	LYS161
A	HIS197
B	HIS77
B	HIS79

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P25910

Chain	Residue	Details
A	ASN167
B	ASN167
C	ASN167
D	ASN167

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