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Iron in PDB 1muy: Catalytic Domain of Muty From Escherichia Coli

Protein crystallography data

The structure of Catalytic Domain of Muty From Escherichia Coli, PDB code: 1muy was solved by Y.Guan, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 83.060, 48.950, 69.030, 90.00, 123.37, 90.00
R / Rfree (%) 15.3 / 23.1

Iron Binding Sites:

The binding sites of Iron atom in the Catalytic Domain of Muty From Escherichia Coli (pdb code 1muy). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Catalytic Domain of Muty From Escherichia Coli, PDB code: 1muy:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1muy

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Iron binding site 1 out of 4 in the Catalytic Domain of Muty From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Catalytic Domain of Muty From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:17.4
occ:1.00
FE1 A:SF4300 0.0 17.4 1.0
S2 A:SF4300 2.2 19.0 1.0
S3 A:SF4300 2.2 20.2 1.0
SG A:CYS202 2.3 17.9 1.0
S4 A:SF4300 2.3 19.9 1.0
FE2 A:SF4300 2.7 17.8 1.0
FE4 A:SF4300 2.7 18.4 1.0
FE3 A:SF4300 2.7 22.8 1.0
CB A:CYS202 3.0 18.9 1.0
S1 A:SF4300 3.9 20.8 1.0
CB A:LEU204 4.4 19.9 1.0
CA A:CYS202 4.5 18.8 1.0
SG A:CYS192 4.6 21.1 1.0
CB A:CYS192 4.7 19.4 1.0
CA A:CYS199 4.7 19.6 1.0
SG A:CYS208 4.8 19.9 1.0
SG A:CYS199 4.8 23.0 1.0
N A:GLN205 4.9 18.3 1.0
C A:LEU204 4.9 18.0 1.0
CB A:CYS208 4.9 19.0 1.0
CB A:CYS199 4.9 21.4 1.0

Iron binding site 2 out of 4 in 1muy

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Iron binding site 2 out of 4 in the Catalytic Domain of Muty From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Catalytic Domain of Muty From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:17.8
occ:1.00
FE2 A:SF4300 0.0 17.8 1.0
S1 A:SF4300 2.2 20.8 1.0
S4 A:SF4300 2.2 19.9 1.0
SG A:CYS192 2.3 21.1 1.0
S3 A:SF4300 2.3 20.2 1.0
FE1 A:SF4300 2.7 17.4 1.0
FE4 A:SF4300 2.7 18.4 1.0
FE3 A:SF4300 2.7 22.8 1.0
CB A:CYS192 3.2 19.4 1.0
S2 A:SF4300 3.8 19.0 1.0
CA A:CYS192 3.9 19.0 1.0
CD A:ARG147 4.1 19.1 1.0
CB A:PRO197 4.4 19.6 1.0
CB A:ARG147 4.4 16.5 1.0
NH1 A:ARG147 4.6 20.2 1.0
SG A:CYS202 4.7 17.9 1.0
SG A:CYS199 4.7 23.0 1.0
SG A:CYS208 4.8 19.9 1.0
CG A:ARG147 4.9 18.3 1.0
CG A:PRO197 4.9 21.1 1.0
N A:CYS192 4.9 19.9 1.0
C A:CYS192 5.0 21.0 1.0

Iron binding site 3 out of 4 in 1muy

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Iron binding site 3 out of 4 in the Catalytic Domain of Muty From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Catalytic Domain of Muty From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:22.8
occ:1.00
FE3 A:SF4300 0.0 22.8 1.0
SG A:CYS199 2.2 23.0 1.0
S1 A:SF4300 2.3 20.8 1.0
S2 A:SF4300 2.3 19.0 1.0
S4 A:SF4300 2.3 19.9 1.0
FE4 A:SF4300 2.7 18.4 1.0
FE2 A:SF4300 2.7 17.8 1.0
FE1 A:SF4300 2.7 17.4 1.0
CB A:CYS199 3.1 21.4 1.0
CA A:CYS199 3.5 19.6 1.0
S3 A:SF4300 3.9 20.2 1.0
N A:CYS199 4.2 19.1 1.0
CB A:PRO197 4.2 19.6 1.0
CG A:PRO197 4.4 21.1 1.0
CB A:ALA211 4.5 25.7 1.0
SG A:CYS208 4.6 19.9 1.0
CB A:CYS202 4.6 18.9 1.0
SG A:CYS192 4.8 21.1 1.0
SG A:CYS202 4.8 17.9 1.0
C A:CYS199 4.8 17.0 1.0
O A:CYS199 5.0 19.7 1.0
C A:LYS198 5.0 19.4 1.0

Iron binding site 4 out of 4 in 1muy

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Iron binding site 4 out of 4 in the Catalytic Domain of Muty From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Catalytic Domain of Muty From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:18.4
occ:1.00
FE4 A:SF4300 0.0 18.4 1.0
S2 A:SF4300 2.2 19.0 1.0
SG A:CYS208 2.3 19.9 1.0
S3 A:SF4300 2.3 20.2 1.0
S1 A:SF4300 2.3 20.8 1.0
FE3 A:SF4300 2.7 22.8 1.0
FE1 A:SF4300 2.7 17.4 1.0
FE2 A:SF4300 2.7 17.8 1.0
CB A:CYS208 3.2 19.0 1.0
S4 A:SF4300 3.8 19.9 1.0
CB A:ALA211 4.3 25.7 1.0
N A:ALA211 4.4 17.9 1.0
CB A:ARG147 4.4 16.5 1.0
SG A:CYS199 4.6 23.0 1.0
CA A:CYS208 4.6 19.2 1.0
N A:CYS148 4.8 18.5 1.0
SG A:CYS202 4.8 17.9 1.0
SG A:CYS192 4.8 21.1 1.0
CA A:ALA211 4.9 22.8 1.0
CB A:ALA210 4.9 19.6 1.0
C A:ARG147 5.0 18.3 1.0
CA A:CYS148 5.0 17.9 1.0

Reference:

Y.Guan, R.C.Manuel, A.S.Arvai, S.S.Parikh, C.D.Mol, J.H.Miller, S.Lloyd, J.A.Tainer. Muty Catalytic Core, Mutant and Bound Adenine Structures Define Specificity For Dna Repair Enzyme Superfamily. Nat.Struct.Biol. V. 5 1058 1998.
ISSN: ISSN 1072-8368
PubMed: 9846876
DOI: 10.1038/4168
Page generated: Wed Jul 16 18:18:37 2025

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