5HH4

Crystal structure of metallo-beta-lactamase IMP-1 in complex with a phosphonate-based inhibitor

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	HOH422

---

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

Chain	Residue
A	60M303
A	HOH422
A	ASP81
A	CYS158
A	HIS197
A	ZN301

---

site_id	AC3
Number of Residues	15
Details	binding site for residue 60M A 303

Chain	Residue
A	VAL25
A	HIS79
A	SER80
A	ASP81
A	HIS139
A	CYS158
A	LYS161
A	GLY166
A	ASN167
A	HIS197
A	ZN302
A	HOH422
A	HOH433
A	HOH435
D	EDO303

---

site_id	AC4
Number of Residues	6
Details	binding site for residue ZN B 301

Chain	Residue
B	ASP81
B	CYS158
B	HIS197
B	ZN302
B	60M303
B	HOH479

---

site_id	AC5
Number of Residues	5
Details	binding site for residue ZN B 302

Chain	Residue
B	HIS77
B	HIS79
B	HIS139
B	ZN301
B	HOH479

---

site_id	AC6
Number of Residues	14
Details	binding site for residue 60M B 303

Chain	Residue
B	VAL25
B	HIS79
B	SER80
B	ASP81
B	HIS139
B	CYS158
B	LYS161
B	GLY166
B	ASN167
B	HIS197
B	ZN301
B	HOH479
B	HOH494
B	HOH499

---

site_id	AC7
Number of Residues	6
Details	binding site for residue CL B 304

Chain	Residue
B	GLU43
B	THR52
B	LYS54
B	LYS69
B	HOH430
B	HOH545

---

site_id	AC8
Number of Residues	9
Details	binding site for residue EDO B 305

Chain	Residue
B	SER198
B	GLU199
B	HOH418
C	VAL200
C	GLY201
C	ASP202
C	SER204
C	LEU205
C	HOH414

---

site_id	AC9
Number of Residues	5
Details	binding site for residue ZN C 301

Chain	Residue
C	HIS77
C	HIS79
C	HIS139
C	ZN302
C	HOH524

---

site_id	AD1
Number of Residues	6
Details	binding site for residue ZN C 302

Chain	Residue
C	ASP81
C	CYS158
C	HIS197
C	ZN301
C	HOH465
C	HOH524

---

site_id	AD2
Number of Residues	6
Details	binding site for residue EDO C 303

Chain	Residue
C	GLU14
C	GLY15
C	VAL38
C	LEU39
C	GLU150
C	HOH416

---

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

Chain	Residue
D	HIS77
D	HIS79
D	HIS139
D	ZN302
D	HOH456

---

site_id	AD4
Number of Residues	6
Details	binding site for residue ZN D 302

Chain	Residue
D	ASP81
D	CYS158
D	HIS197
D	ZN301
D	HOH456
D	HOH458

---

site_id	AD5
Number of Residues	4
Details	binding site for residue EDO D 303

Chain	Residue
A	HIS197
A	60M303
D	GLU199
D	HOH422

---

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
B	HIS79
B	ASP81
B	HIS139
B	CYS158
B	LYS161
B	HIS197
C	HIS77
C	HIS79
C	ASP81
C	HIS139
C	CYS158
C	LYS161
C	HIS197
D	HIS77
D	HIS79
D	ASP81
D	HIS139
D	CYS158
D	LYS161
D	HIS197
A	HIS77
A	HIS79
A	ASP81
A	HIS139
A	CYS158
A	LYS161
A	HIS197
B	HIS77

---

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

---