6MGY

Crystal Structure of the New Deli Metallo Beta Lactamase Variant 5 from Klebsiella pneumoniae

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	HIS120
A	HIS122
A	HIS189
A	ZN302
A	HOH484

---

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

Chain	Residue
A	HOH484
A	HOH533
A	ASP124
A	CYS208
A	HIS250
A	ZN301

---

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

Chain	Residue
A	GLY222
A	ALA224
A	HOH503
D	GLY222
D	ALA224
D	HOH432

---

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN B 301

Chain	Residue
B	HIS120
B	HIS122
B	HIS189
B	HOH465

---

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

Chain	Residue
B	ASP124
B	CYS208
B	HIS250
B	HOH465
B	HOH527

---

site_id	AC6
Number of Residues	8
Details	binding site for residue GOL B 303

Chain	Residue
A	PRO150
B	GLY237
B	ALA238
B	ARG256
B	THR260
B	HOH415
B	HOH416
B	HOH433

---

site_id	AC7
Number of Residues	5
Details	binding site for residue K B 304

Chain	Residue
B	GLY222
B	ALA224
B	HOH521
C	GLY222
C	ALA224

---

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

Chain	Residue
C	HIS120
C	HIS122
C	HIS189
C	ZN302
C	HOH413

---

site_id	AC9
Number of Residues	6
Details	binding site for residue ZN C 302

Chain	Residue
C	ASP124
C	CYS208
C	HIS250
C	ZN301
C	HOH413
C	HOH549

---

site_id	AD1
Number of Residues	6
Details	binding site for residue ZN D 301

Chain	Residue
D	ASP124
D	CYS208
D	HIS250
D	ZN302
D	HOH426
D	HOH500

---

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

Chain	Residue
D	HIS120
D	HIS122
D	HIS189
D	ZN301
D	HOH426

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269|PubMed:22713171, ECO:0000269|PubMed:25815530

Chain	Residue	Details
B	ASP124
B	HIS189
B	CYS208
B	HIS250
C	HIS120
C	HIS122
C	ASP124
C	HIS189
C	CYS208
C	HIS250
D	HIS120
D	HIS122
D	ASP124
D	HIS189
D	CYS208
D	HIS250
A	HIS120
A	HIS122
A	ASP124
A	HIS189
A	CYS208
A	HIS250
B	HIS120
B	HIS122

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:22713171

Chain	Residue	Details
C	LYS211
C	ASN220
D	LYS211
D	ASN220
A	LYS211
A	ASN220
B	LYS211
B	ASN220

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