1V14

Crystal Structure of the Colicin E9, mutant His103Ala, in complex with Mg+2 and dsDNA (resolution 2.9A)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004519	molecular_function	endonuclease activity
A	0005102	molecular_function	signaling receptor binding
A	0009617	biological_process	response to bacterium
A	0019835	biological_process	cytolysis
B	0004519	molecular_function	endonuclease activity
B	0005102	molecular_function	signaling receptor binding
B	0009617	biological_process	response to bacterium
B	0019835	biological_process	cytolysis
C	0004519	molecular_function	endonuclease activity
C	0005102	molecular_function	signaling receptor binding
C	0009617	biological_process	response to bacterium
C	0019835	biological_process	cytolysis
D	0004519	molecular_function	endonuclease activity
D	0005102	molecular_function	signaling receptor binding
D	0009617	biological_process	response to bacterium
D	0019835	biological_process	cytolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A1134

Chain	Residue
A	HIS102
A	HIS127
E	DT5
E	DC6

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C1134

Chain	Residue
C	HIS102
C	HIS127
I	DT5
I	DC6

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG E1009

Chain	Residue
L	DG9
L	DC10
E	DG3

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG G1009

Chain	Residue
G	DG3
J	DC10

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG I1009

Chain	Residue
H	DC10
I	DG3

---

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG K1009

Chain	Residue
F	DC10
K	DG3

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	128
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	44
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	52
Details	Compositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 791

Chain	Residue	Details
A	ARG5	electrostatic stabiliser
A	ARG96	electrostatic stabiliser
A	GLU100	electrostatic stabiliser
A	HIS102	metal ligand
A	ALA103	increase nucleophilicity, proton acceptor, proton donor
A	HIS127	metal ligand
A	HIS131	metal ligand

---

site_id	MCSA2
Number of Residues	7
Details	M-CSA 791

Chain	Residue	Details
B	ARG5	electrostatic stabiliser
B	ARG96	electrostatic stabiliser
B	GLU100	electrostatic stabiliser
B	HIS102	metal ligand
B	ALA103	increase nucleophilicity, proton acceptor, proton donor
B	HIS127	metal ligand
B	HIS131	metal ligand

---

site_id	MCSA3
Number of Residues	7
Details	M-CSA 791

Chain	Residue	Details
C	ARG5	electrostatic stabiliser
C	ARG96	electrostatic stabiliser
C	GLU100	electrostatic stabiliser
C	HIS102	metal ligand
C	ALA103	increase nucleophilicity, proton acceptor, proton donor
C	HIS127	metal ligand
C	HIS131	metal ligand

---

site_id	MCSA4
Number of Residues	7
Details	M-CSA 791

Chain	Residue	Details
D	ARG5	electrostatic stabiliser
D	ARG96	electrostatic stabiliser
D	GLU100	electrostatic stabiliser
D	HIS102	metal ligand
D	ALA103	increase nucleophilicity, proton acceptor, proton donor
D	HIS127	metal ligand
D	HIS131	metal ligand

---