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Iron in PDB 1kg6: Crystal Structure of the K142R Mutant of E.Coli Muty (Core Fragment)

Protein crystallography data

The structure of Crystal Structure of the K142R Mutant of E.Coli Muty (Core Fragment), PDB code: 1kg6 was solved by R.Gilboa, A.Kilshtein, D.O.Zharkov, J.H.Kycia, S.E.Gerchman, A.P.Grollman, G.Shoham, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.00 / 1.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 82.730, 49.950, 69.660, 90.00, 122.74, 90.00
R / Rfree (%) 15.5 / 19.6

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the K142R Mutant of E.Coli Muty (Core Fragment) (pdb code 1kg6). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of the K142R Mutant of E.Coli Muty (Core Fragment), PDB code: 1kg6:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1kg6

Go back to Iron Binding Sites List in 1kg6
Iron binding site 1 out of 4 in the Crystal Structure of the K142R Mutant of E.Coli Muty (Core Fragment)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of the K142R Mutant of E.Coli Muty (Core Fragment) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:10.8
occ:1.00
FE1 A:SF4300 0.0 10.8 1.0
SG A:CYS202 2.3 11.4 1.0
S2 A:SF4300 2.3 11.8 1.0
S3 A:SF4300 2.3 11.7 1.0
S4 A:SF4300 2.3 11.7 1.0
FE2 A:SF4300 2.7 11.2 1.0
FE4 A:SF4300 2.7 11.1 1.0
FE3 A:SF4300 2.8 11.7 1.0
CB A:CYS202 3.0 12.7 1.0
S1 A:SF4300 3.9 11.8 1.0
CB A:LEU204 4.4 11.5 1.0
CA A:CYS202 4.5 9.1 1.0
SG A:CYS192 4.7 13.0 1.0
CB A:CYS192 4.7 10.0 1.0
N A:GLN205 4.8 11.8 1.0
CA A:CYS199 4.8 9.4 1.0
SG A:CYS208 4.9 11.7 1.0
SG A:CYS199 4.9 12.8 1.0
C A:LEU204 4.9 11.3 1.0
N A:LEU204 5.0 11.6 1.0
CD1 A:LEU204 5.0 19.0 1.0

Iron binding site 2 out of 4 in 1kg6

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Iron binding site 2 out of 4 in the Crystal Structure of the K142R Mutant of E.Coli Muty (Core Fragment)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of the K142R Mutant of E.Coli Muty (Core Fragment) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:11.2
occ:1.00
FE2 A:SF4300 0.0 11.2 1.0
S3 A:SF4300 2.3 11.7 1.0
SG A:CYS192 2.3 13.0 1.0
S1 A:SF4300 2.3 11.8 1.0
S4 A:SF4300 2.3 11.7 1.0
FE1 A:SF4300 2.7 10.8 1.0
FE4 A:SF4300 2.7 11.1 1.0
FE3 A:SF4300 2.8 11.7 1.0
CB A:CYS192 3.2 10.0 1.0
S2 A:SF4300 3.9 11.8 1.0
CA A:CYS192 4.0 9.6 1.0
CD A:ARG147 4.2 10.4 1.0
CB A:ARG147 4.4 10.1 1.0
CB A:PRO197 4.6 13.2 1.0
SG A:CYS202 4.7 11.4 1.0
NH1 A:ARG147 4.8 12.0 1.0
SG A:CYS199 4.9 12.8 1.0
SG A:CYS208 4.9 11.7 1.0
CG A:ARG147 5.0 7.7 1.0
N A:CYS192 5.0 11.6 1.0

Iron binding site 3 out of 4 in 1kg6

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Iron binding site 3 out of 4 in the Crystal Structure of the K142R Mutant of E.Coli Muty (Core Fragment)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of the K142R Mutant of E.Coli Muty (Core Fragment) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:11.7
occ:1.00
FE3 A:SF4300 0.0 11.7 1.0
S4 A:SF4300 2.2 11.7 1.0
S2 A:SF4300 2.3 11.8 1.0
S1 A:SF4300 2.3 11.8 1.0
SG A:CYS199 2.3 12.8 1.0
FE4 A:SF4300 2.7 11.1 1.0
FE1 A:SF4300 2.8 10.8 1.0
FE2 A:SF4300 2.8 11.2 1.0
CB A:CYS199 3.3 14.1 1.0
CA A:CYS199 3.6 9.4 1.0
S3 A:SF4300 3.9 11.7 1.0
N A:CYS199 4.2 10.3 1.0
CB A:PRO197 4.3 13.2 1.0
CB A:ALA211 4.5 16.8 1.0
CG A:PRO197 4.6 17.0 1.0
CB A:CYS202 4.6 12.7 1.0
SG A:CYS208 4.7 11.7 1.0
SG A:CYS202 4.8 11.4 1.0
C A:CYS199 4.9 11.2 1.0
SG A:CYS192 4.9 13.0 1.0

Iron binding site 4 out of 4 in 1kg6

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Iron binding site 4 out of 4 in the Crystal Structure of the K142R Mutant of E.Coli Muty (Core Fragment)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of the K142R Mutant of E.Coli Muty (Core Fragment) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:11.1
occ:1.00
FE4 A:SF4300 0.0 11.1 1.0
S3 A:SF4300 2.2 11.7 1.0
S2 A:SF4300 2.3 11.8 1.0
S1 A:SF4300 2.3 11.8 1.0
SG A:CYS208 2.4 11.7 1.0
FE3 A:SF4300 2.7 11.7 1.0
FE1 A:SF4300 2.7 10.8 1.0
FE2 A:SF4300 2.7 11.2 1.0
CB A:CYS208 3.3 12.7 1.0
S4 A:SF4300 3.9 11.7 1.0
CB A:ALA211 4.4 16.8 1.0
CB A:ARG147 4.5 10.1 1.0
N A:ALA211 4.6 12.7 1.0
N A:CYS148 4.7 11.6 1.0
SG A:CYS199 4.7 12.8 1.0
CA A:CYS208 4.7 10.4 1.0
SG A:CYS202 4.8 11.4 1.0
CA A:CYS148 4.8 11.2 1.0
SG A:CYS192 4.9 13.0 1.0
C A:ARG147 4.9 9.5 1.0
CB A:ALA210 5.0 10.8 1.0

Reference:

R.Gilboa, A.Kilshtein, D.O.Zharkov, J.H.Kycia, S.E.Gerchman, A.P.Grollman, G.Shoham. Analysis of the E.Coli Muty Dna Glycosylase Structure and Function By Site-Directed Mutagenesis To Be Published.
Page generated: Sat Aug 3 09:12:30 2024

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