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Iron in PDB 4f28: The Crystal Structure of A Human Mitoneet Mutant with Met 62 Replaced By A Gly

Protein crystallography data

The structure of The Crystal Structure of A Human Mitoneet Mutant with Met 62 Replaced By A Gly, PDB code: 4f28 was solved by E.L.Baxter, J.A.Zuris, C.Wang, H.L.Axelrod, A.E.Cohen, M.L.Paddock, R.Nechushtai, J.N.Onuchic, P.A.Jennings, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.87 / 1.55
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.330, 56.600, 59.110, 90.00, 90.00, 90.00
R / Rfree (%) 21.6 / 24.9

Iron Binding Sites:

The binding sites of Iron atom in the The Crystal Structure of A Human Mitoneet Mutant with Met 62 Replaced By A Gly (pdb code 4f28). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the The Crystal Structure of A Human Mitoneet Mutant with Met 62 Replaced By A Gly, PDB code: 4f28:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 4f28

Go back to Iron Binding Sites List in 4f28
Iron binding site 1 out of 4 in the The Crystal Structure of A Human Mitoneet Mutant with Met 62 Replaced By A Gly


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Crystal Structure of A Human Mitoneet Mutant with Met 62 Replaced By A Gly within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:39.0
occ:1.00
FE1 A:FES201 0.0 39.0 1.0
S1 A:FES201 2.2 42.1 1.0
S2 A:FES201 2.2 38.2 1.0
SG A:CYS74 2.2 40.3 1.0
SG A:CYS72 2.4 38.2 1.0
FE2 A:FES201 2.7 41.0 1.0
CB A:CYS72 3.4 35.4 1.0
CB A:CYS74 3.4 36.8 1.0
N A:CYS74 3.6 34.1 1.0
CA A:CYS72 3.8 34.3 1.0
CA A:CYS74 4.0 35.0 1.0
N A:ARG73 4.0 32.7 1.0
CB A:HIS87 4.1 41.2 1.0
N A:HIS87 4.2 45.4 1.0
ND1 A:HIS87 4.2 43.7 1.0
C A:CYS72 4.3 35.8 1.0
CB A:SER77 4.4 43.2 1.0
N A:SER77 4.4 42.5 1.0
N A:TRP75 4.4 36.6 1.0
C A:CYS74 4.5 37.8 1.0
CA A:HIS87 4.5 43.5 1.0
SG A:CYS83 4.6 44.4 1.0
CG A:HIS87 4.7 43.5 1.0
N A:ARG76 4.7 43.8 1.0
C A:ARG73 4.7 35.0 1.0
CA A:CYS83 4.8 41.1 1.0
CA A:SER77 4.9 42.8 1.0
CB A:CYS83 4.9 40.8 1.0
CA A:ARG73 5.0 31.8 1.0

Iron binding site 2 out of 4 in 4f28

Go back to Iron Binding Sites List in 4f28
Iron binding site 2 out of 4 in the The Crystal Structure of A Human Mitoneet Mutant with Met 62 Replaced By A Gly


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Crystal Structure of A Human Mitoneet Mutant with Met 62 Replaced By A Gly within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:41.0
occ:1.00
FE2 A:FES201 0.0 41.0 1.0
ND1 A:HIS87 2.1 43.7 1.0
S1 A:FES201 2.2 42.1 1.0
SG A:CYS83 2.2 44.4 1.0
S2 A:FES201 2.2 38.2 1.0
FE1 A:FES201 2.7 39.0 1.0
CE1 A:HIS87 3.0 45.5 1.0
CG A:HIS87 3.2 43.5 1.0
CB A:CYS83 3.3 40.8 1.0
CB A:HIS87 3.6 41.2 1.0
CA A:CYS83 3.9 41.1 1.0
N A:GLY85 4.0 50.9 1.0
N A:HIS87 4.0 45.4 1.0
NE2 A:HIS87 4.2 45.8 1.0
CD A:PRO100 4.3 37.8 1.0
CD2 A:HIS87 4.3 45.4 1.0
CA A:GLY85 4.3 50.8 1.0
N A:ASP84 4.3 48.2 1.0
CB A:PRO100 4.3 38.1 1.0
SG A:CYS74 4.4 40.3 1.0
CA A:HIS87 4.5 43.5 1.0
N A:ALA86 4.5 50.7 1.0
C A:CYS83 4.5 49.7 1.0
CG A:PRO100 4.6 43.0 1.0
SG A:CYS72 4.6 38.2 1.0
CA A:CYS72 4.6 34.3 1.0
C A:GLY85 4.6 54.7 1.0
CB A:CYS72 4.7 35.4 1.0
N A:PRO100 4.7 35.1 1.0
CA A:PRO100 5.0 35.3 1.0

Iron binding site 3 out of 4 in 4f28

Go back to Iron Binding Sites List in 4f28
Iron binding site 3 out of 4 in the The Crystal Structure of A Human Mitoneet Mutant with Met 62 Replaced By A Gly


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of The Crystal Structure of A Human Mitoneet Mutant with Met 62 Replaced By A Gly within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe201

b:34.6
occ:1.00
FE1 B:FES201 0.0 34.6 1.0
S1 B:FES201 2.2 37.6 1.0
S2 B:FES201 2.2 33.9 1.0
SG B:CYS74 2.3 36.1 1.0
SG B:CYS72 2.3 34.2 1.0
FE2 B:FES201 2.7 36.4 1.0
CB B:CYS72 3.3 30.3 1.0
CB B:CYS74 3.4 31.6 1.0
N B:CYS74 3.5 30.9 1.0
CA B:CYS72 3.7 30.6 1.0
N B:ARG73 3.9 31.2 1.0
CA B:CYS74 3.9 30.8 1.0
CB B:HIS87 4.1 35.3 1.0
N B:HIS87 4.2 38.6 1.0
C B:CYS72 4.2 33.3 1.0
ND1 B:HIS87 4.3 39.5 1.0
N B:TRP75 4.4 32.5 1.0
CB B:SER77 4.4 42.4 1.0
N B:SER77 4.4 39.9 1.0
C B:CYS74 4.5 33.0 1.0
CA B:HIS87 4.5 37.4 1.0
C B:ARG73 4.6 32.8 1.0
SG B:CYS83 4.7 39.0 1.0
N B:ARG76 4.7 37.0 1.0
CG B:HIS87 4.7 38.1 1.0
CA B:CYS83 4.8 36.5 1.0
CB B:CYS83 4.9 35.2 1.0
CA B:ARG73 4.9 30.1 1.0
CA B:SER77 5.0 40.4 1.0

Iron binding site 4 out of 4 in 4f28

Go back to Iron Binding Sites List in 4f28
Iron binding site 4 out of 4 in the The Crystal Structure of A Human Mitoneet Mutant with Met 62 Replaced By A Gly


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of The Crystal Structure of A Human Mitoneet Mutant with Met 62 Replaced By A Gly within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe201

b:36.4
occ:1.00
FE2 B:FES201 0.0 36.4 1.0
ND1 B:HIS87 2.1 39.5 1.0
S1 B:FES201 2.2 37.6 1.0
S2 B:FES201 2.2 33.9 1.0
SG B:CYS83 2.3 39.0 1.0
FE1 B:FES201 2.7 34.6 1.0
CE1 B:HIS87 3.0 40.2 1.0
CG B:HIS87 3.2 38.1 1.0
CB B:CYS83 3.3 35.2 1.0
CB B:HIS87 3.6 35.3 1.0
CA B:CYS83 3.9 36.5 1.0
N B:HIS87 3.9 38.6 1.0
N B:GLY85 4.1 45.8 1.0
NE2 B:HIS87 4.2 41.6 1.0
CD B:PRO100 4.3 33.7 1.0
CD2 B:HIS87 4.3 41.4 1.0
CA B:GLY85 4.3 45.3 1.0
CB B:PRO100 4.3 33.7 1.0
CA B:HIS87 4.3 37.4 1.0
N B:ASP84 4.4 43.7 1.0
N B:ALA86 4.4 44.5 1.0
SG B:CYS74 4.4 36.1 1.0
C B:CYS83 4.5 45.5 1.0
C B:GLY85 4.5 47.9 1.0
CG B:PRO100 4.5 38.4 1.0
SG B:CYS72 4.6 34.2 1.0
CA B:CYS72 4.6 30.6 1.0
CB B:CYS72 4.7 30.3 1.0
N B:PRO100 4.7 31.1 1.0
CA B:PRO100 5.0 30.3 1.0
C B:ALA86 5.0 43.3 1.0

Reference:

E.L.Baxter, J.A.Zuris, C.Wang, P.L.Vo, H.L.Axelrod, A.E.Cohen, M.L.Paddock, R.Nechushtai, J.N.Onuchic, P.A.Jennings. Allosteric Control in A Metalloprotein Dramatically Alters Function. Proc.Natl.Acad.Sci.Usa V. 110 948 2013.
ISSN: ISSN 0027-8424
PubMed: 23271805
DOI: 10.1073/PNAS.1208286110
Page generated: Mon Aug 5 01:50:58 2024

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