5EV6

Crystal structure of the native, di-zinc metallo-beta-lactamase IMP-1

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	HOH478

---

site_id	AC2
Number of Residues	6
Details	binding site for residue ZN A 302

Chain	Residue
A	HOH426
A	HOH478
A	ASP81
A	CYS158
A	HIS197
A	ZN301

---

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

Chain	Residue
A	GLU14
A	GLY15
A	LEU39
A	GLU150
A	ARG151
A	HOH438

---

site_id	AC4
Number of Residues	9
Details	binding site for residue ACT A 304

Chain	Residue
A	SER99
A	PHE118
A	SER119
A	GLY120
A	TYR134
A	VAL144
A	HOH413
A	HOH495
A	HOH498

---

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

Chain	Residue
B	HIS77
B	HIS79
B	HIS139
B	ZN302
B	HOH476

---

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

Chain	Residue
B	ASP81
B	CYS158
B	HIS197
B	ZN301
B	HOH476

---

site_id	AC7
Number of Residues	6
Details	binding site for residue EDO B 303

Chain	Residue
B	GLU14
B	VAL38
B	LEU39
B	GLU150
B	ARG151
B	HOH444

---

site_id	AC8
Number of Residues	5
Details	binding site for residue ZN C 301

Chain	Residue
C	ASP81
C	CYS158
C	HIS197
C	ZN302
C	HOH515

---

site_id	AC9
Number of Residues	5
Details	binding site for residue ZN C 302

Chain	Residue
C	HIS77
C	HIS79
C	HIS139
C	ZN301
C	HOH515

---

site_id	AD1
Number of Residues	5
Details	binding site for residue ZN D 301

Chain	Residue
D	HIS77
D	HIS79
D	HIS139
D	ZN302
D	HOH429

---

site_id	AD2
Number of Residues	5
Details	binding site for residue ZN D 302

Chain	Residue
D	ASP81
D	CYS158
D	HIS197
D	ZN301
D	HOH429

---

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 site: {"evidences":[{"source":"PubMed","id":"26482303","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P25910","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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