Iron in PDB 4f1e: The Crystal Structure of A Human Mitoneet Mutant with Asp 67 Replaced By A Gly

The structure of The Crystal Structure of A Human Mitoneet Mutant with Asp 67 Replaced By A Gly, PDB code: 4f1e was solved by E.I.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)	49.54 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.396, 110.855, 207.294, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 22.7

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 36;

Binding sites:

The binding sites of Iron atom in the The Crystal Structure of A Human Mitoneet Mutant with Asp 67 Replaced By A Gly (pdb code 4f1e). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 36 binding sites of Iron where determined in the The Crystal Structure of A Human Mitoneet Mutant with Asp 67 Replaced By A Gly, PDB code: 4f1e:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 36 in the The Crystal Structure of A Human Mitoneet Mutant with Asp 67 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 Asp 67 Replaced By A Gly within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:43.0 occ:1.00 FE1 A:FES201 0.0 43.0 1.0 S1 A:FES201 2.2 44.8 1.0 S2 A:FES201 2.2 41.8 1.0 SG A:CYS72 2.2 46.2 1.0 SG A:CYS74 2.3 42.6 1.0 FE2 A:FES201 2.8 43.1 1.0 CB A:CYS72 3.2 41.3 1.0 CB A:CYS74 3.4 39.7 1.0 N A:CYS74 3.4 40.0 1.0 CA A:CYS72 3.5 39.9 1.0 N A:ARG73 3.7 37.7 1.0 CA A:CYS74 3.9 41.0 1.0 C A:CYS72 4.1 42.3 1.0 CB A:HIS87 4.2 42.7 1.0 N A:TRP75 4.3 49.5 1.0 ND1 A:HIS87 4.4 45.4 1.0 N A:HIS87 4.4 45.1 1.0 C A:CYS74 4.4 52.0 1.0 CB A:SER77 4.5 48.8 1.0 C A:ARG73 4.5 43.2 1.0 N A:SER77 4.6 49.8 1.0 N A:ARG76 4.7 52.1 1.0 CA A:HIS87 4.7 44.7 1.0 CA A:CYS83 4.8 40.4 1.0 SG A:CYS83 4.8 45.1 1.0 CA A:ARG73 4.8 37.5 1.0 CG A:HIS87 4.8 45.0 1.0 CB A:CYS83 4.8 40.2 1.0 N A:CYS72 4.9 39.8 1.0

Iron binding site 2 out of 36 in the The Crystal Structure of A Human Mitoneet Mutant with Asp 67 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 Asp 67 Replaced By A Gly within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:43.1 occ:1.00 FE2 A:FES201 0.0 43.1 1.0 ND1 A:HIS87 2.2 45.4 1.0 S1 A:FES201 2.2 44.8 1.0 S2 A:FES201 2.3 41.8 1.0 SG A:CYS83 2.3 45.1 1.0 FE1 A:FES201 2.8 43.0 1.0 CE1 A:HIS87 3.1 45.0 1.0 CB A:CYS83 3.2 40.2 1.0 CG A:HIS87 3.3 45.0 1.0 CB A:HIS87 3.7 42.7 1.0 CA A:CYS83 3.8 40.4 1.0 N A:GLY85 3.9 47.6 1.0 N A:HIS87 4.0 45.1 1.0 CA A:GLY85 4.2 47.8 1.0 N A:ASP84 4.2 45.1 1.0 NE2 A:HIS87 4.3 46.3 1.0 CB A:PRO100 4.3 41.9 1.0 N A:ALA86 4.3 49.4 1.0 CD A:PRO100 4.4 42.1 1.0 CD2 A:HIS87 4.4 46.8 1.0 C A:CYS83 4.4 45.8 1.0 C A:GLY85 4.5 52.2 1.0 CA A:HIS87 4.5 44.7 1.0 SG A:CYS74 4.5 42.6 1.0 CG A:PRO100 4.5 46.4 1.0 CA A:CYS72 4.6 39.9 1.0 CB A:CYS72 4.7 41.3 1.0 SG A:CYS72 4.7 46.2 1.0 N A:PRO100 4.7 41.7 1.0 CA A:PRO100 4.9 40.6 1.0

Iron binding site 3 out of 36 in the The Crystal Structure of A Human Mitoneet Mutant with Asp 67 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 Asp 67 Replaced By A Gly within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:51.5 occ:1.00 FE1 B:FES201 0.0 51.5 1.0 S1 B:FES201 2.2 53.9 1.0 S2 B:FES201 2.2 51.1 1.0 SG B:CYS74 2.3 58.0 1.0 SG B:CYS72 2.3 48.1 1.0 FE2 B:FES201 2.9 53.0 1.0 CB B:CYS72 3.3 42.9 1.0 CB B:CYS74 3.5 53.5 1.0 N B:CYS74 3.5 47.3 1.0 CA B:CYS72 3.7 42.0 1.0 N B:ARG73 3.9 42.8 1.0 CA B:CYS74 3.9 50.8 1.0 CB B:HIS87 4.1 55.3 1.0 C B:CYS72 4.2 44.4 1.0 N B:HIS87 4.3 57.5 1.0 N B:TRP75 4.3 50.6 1.0 ND1 B:HIS87 4.4 58.9 1.0 CB B:SER77 4.4 48.6 1.0 C B:CYS74 4.4 55.8 1.0 N B:SER77 4.4 53.4 1.0 CA B:HIS87 4.6 57.5 1.0 N B:ARG76 4.6 52.4 1.0 C B:ARG73 4.6 48.2 1.0 CG B:HIS87 4.8 58.8 1.0 SG B:CYS83 4.8 53.2 1.0 CA B:CYS83 4.9 47.8 1.0 CA B:ARG73 4.9 42.6 1.0 CA B:SER77 4.9 51.8 1.0 CB B:CYS83 5.0 47.1 1.0 N B:CYS72 5.0 41.2 1.0

Iron binding site 4 out of 36 in the The Crystal Structure of A Human Mitoneet Mutant with Asp 67 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 Asp 67 Replaced By A Gly within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:53.0 occ:1.00 FE2 B:FES201 0.0 53.0 1.0 ND1 B:HIS87 2.2 58.9 1.0 S2 B:FES201 2.2 51.1 1.0 S1 B:FES201 2.3 53.9 1.0 SG B:CYS83 2.3 53.2 1.0 FE1 B:FES201 2.9 51.5 1.0 CE1 B:HIS87 3.0 58.5 1.0 CB B:CYS83 3.2 47.1 1.0 CG B:HIS87 3.3 58.8 1.0 CB B:HIS87 3.7 55.3 1.0 CA B:CYS83 3.8 47.8 1.0 N B:GLY85 4.0 56.5 1.0 N B:HIS87 4.1 57.5 1.0 CB B:PRO100 4.2 46.9 1.0 NE2 B:HIS87 4.2 60.7 1.0 N B:ASP84 4.3 53.2 1.0 CA B:GLY85 4.3 57.7 1.0 CD B:PRO100 4.3 48.9 1.0 CD2 B:HIS87 4.3 61.4 1.0 N B:ALA86 4.4 55.8 1.0 CG B:PRO100 4.4 51.7 1.0 C B:CYS83 4.4 55.0 1.0 CA B:HIS87 4.5 57.5 1.0 C B:GLY85 4.6 61.6 1.0 CA B:CYS72 4.6 42.0 1.0 SG B:CYS74 4.6 58.0 1.0 N B:PRO100 4.6 47.6 1.0 CB B:CYS72 4.7 42.9 1.0 SG B:CYS72 4.7 48.1 1.0 CA B:PRO100 4.8 44.8 1.0

Iron binding site 5 out of 36 in the The Crystal Structure of A Human Mitoneet Mutant with Asp 67 Replaced By A Gly


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of The Crystal Structure of A Human Mitoneet Mutant with Asp 67 Replaced By A Gly within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:64.4 occ:1.00 FE1 C:FES201 0.0 64.4 1.0 S1 C:FES201 2.2 66.5 1.0 S2 C:FES201 2.2 63.1 1.0 SG C:CYS72 2.3 62.2 1.0 SG C:CYS74 2.3 64.8 1.0 FE2 C:FES201 3.0 64.7 1.0 CB C:CYS72 3.2 57.1 1.0 CB C:CYS74 3.5 60.5 1.0 N C:CYS74 3.5 58.9 1.0 CA C:CYS72 3.6 55.1 1.0 N C:ARG73 3.8 54.1 1.0 CA C:CYS74 4.0 60.5 1.0 C C:CYS72 4.1 59.0 1.0 CB C:HIS87 4.2 68.8 1.0 N C:TRP75 4.3 68.7 1.0 N C:HIS87 4.4 73.0 1.0 ND1 C:HIS87 4.4 71.9 1.0 CB C:SER77 4.4 65.2 1.0 C C:CYS74 4.4 70.1 1.0 N C:SER77 4.5 67.6 1.0 N C:ARG76 4.6 71.8 1.0 C C:ARG73 4.6 58.2 1.0 CA C:HIS87 4.7 71.6 1.0 CG C:HIS87 4.8 71.1 1.0 CA C:ARG73 4.9 52.8 1.0 CA C:CYS83 4.9 57.8 1.0 SG C:CYS83 4.9 59.2 1.0 N C:CYS72 5.0 53.3 1.0 CA C:SER77 5.0 67.8 1.0

Iron binding site 6 out of 36 in the The Crystal Structure of A Human Mitoneet Mutant with Asp 67 Replaced By A Gly


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of The Crystal Structure of A Human Mitoneet Mutant with Asp 67 Replaced By A Gly within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:64.7 occ:1.00 FE2 C:FES201 0.0 64.7 1.0 SG C:CYS83 2.2 59.2 1.0 S2 C:FES201 2.2 63.1 1.0 S1 C:FES201 2.2 66.5 1.0 ND1 C:HIS87 2.3 71.9 1.0 FE1 C:FES201 3.0 64.4 1.0 CE1 C:HIS87 3.1 70.7 1.0 CB C:CYS83 3.1 55.3 1.0 CG C:HIS87 3.4 71.1 1.0 CA C:CYS83 3.6 57.8 1.0 CB C:HIS87 3.9 68.8 1.0 N C:GLY85 3.9 73.6 1.0 N C:ASP84 4.1 66.8 1.0 CA C:GLY85 4.2 73.9 1.0 N C:HIS87 4.2 73.0 1.0 CB C:PRO100 4.2 52.0 1.0 C C:CYS83 4.2 66.1 1.0 NE2 C:HIS87 4.3 71.7 1.0 CD C:PRO100 4.3 53.6 1.0 N C:ALA86 4.4 73.8 1.0 CD2 C:HIS87 4.4 72.4 1.0 CG C:PRO100 4.5 56.7 1.0 CA C:CYS72 4.5 55.1 1.0 C C:GLY85 4.5 78.3 1.0 CB C:CYS72 4.6 57.1 1.0 CA C:HIS87 4.7 71.6 1.0 SG C:CYS74 4.7 64.8 1.0 N C:PRO100 4.7 52.0 1.0 SG C:CYS72 4.7 62.2 1.0 CA C:PRO100 4.9 49.9 1.0 N C:CYS83 4.9 57.2 1.0 C C:ASP84 5.0 78.3 1.0

Iron binding site 7 out of 36 in the The Crystal Structure of A Human Mitoneet Mutant with Asp 67 Replaced By A Gly


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of The Crystal Structure of A Human Mitoneet Mutant with Asp 67 Replaced By A Gly within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe500 b:61.3 occ:1.00 FE1 D:FES500 0.0 61.3 1.0 S1 D:FES500 2.2 62.9 1.0 SG D:CYS74 2.2 69.6 1.0 S2 D:FES500 2.2 60.2 1.0 SG D:CYS72 2.4 58.5 1.0 FE2 D:FES500 2.9 61.4 1.0 CB D:CYS74 3.4 65.6 1.0 CB D:CYS72 3.4 52.1 1.0 N D:CYS74 3.5 61.9 1.0 CA D:CYS72 3.8 50.0 1.0 CA D:CYS74 3.9 64.5 1.0 N D:ARG73 3.9 51.8 1.0 CB D:HIS87 4.1 66.4 1.0 N D:HIS87 4.2 70.8 1.0 N D:TRP75 4.2 67.5 1.0 C D:CYS72 4.3 52.6 1.0 C D:CYS74 4.4 73.3 1.0 ND1 D:HIS87 4.4 68.3 1.0 N D:SER77 4.4 63.4 1.0 CB D:SER77 4.5 58.0 1.0 N D:ARG76 4.5 68.7 1.0 CA D:HIS87 4.5 69.8 1.0 C D:ARG73 4.6 61.9 1.0 CG D:HIS87 4.8 68.3 1.0 CA D:ARG73 4.9 52.7 1.0 CB D:ALA86 4.9 71.2 1.0 CA D:SER77 4.9 62.4 1.0 SG D:CYS83 4.9 55.8 1.0 C D:ALA86 5.0 76.4 1.0 CA D:CYS83 5.0 52.5 1.0

Iron binding site 8 out of 36 in the The Crystal Structure of A Human Mitoneet Mutant with Asp 67 Replaced By A Gly


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of The Crystal Structure of A Human Mitoneet Mutant with Asp 67 Replaced By A Gly within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe500 b:61.4 occ:1.00 FE2 D:FES500 0.0 61.4 1.0 ND1 D:HIS87 2.2 68.3 1.0 S1 D:FES500 2.2 62.9 1.0 S2 D:FES500 2.2 60.2 1.0 SG D:CYS83 2.3 55.8 1.0 FE1 D:FES500 2.9 61.3 1.0 CE1 D:HIS87 3.1 67.9 1.0 CB D:CYS83 3.2 51.1 1.0 CG D:HIS87 3.3 68.3 1.0 CB D:HIS87 3.7 66.4 1.0 CA D:CYS83 3.8 52.5 1.0 N D:GLY85 4.1 66.6 1.0 N D:HIS87 4.1 70.8 1.0 CB D:PRO100 4.1 50.8 1.0 NE2 D:HIS87 4.3 69.5 1.0 CD D:PRO100 4.3 53.6 1.0 N D:ASP84 4.3 58.9 1.0 CA D:GLY85 4.3 67.8 1.0 CD2 D:HIS87 4.4 70.4 1.0 CG D:PRO100 4.4 56.4 1.0 C D:CYS83 4.5 59.8 1.0 N D:ALA86 4.5 69.8 1.0 CA D:CYS72 4.5 50.0 1.0 CA D:HIS87 4.6 69.8 1.0 SG D:CYS74 4.6 69.6 1.0 N D:PRO100 4.6 52.9 1.0 C D:GLY85 4.6 74.7 1.0 CB D:CYS72 4.7 52.1 1.0 CA D:PRO100 4.7 49.2 1.0 SG D:CYS72 4.7 58.5 1.0

Iron binding site 9 out of 36 in the The Crystal Structure of A Human Mitoneet Mutant with Asp 67 Replaced By A Gly


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of The Crystal Structure of A Human Mitoneet Mutant with Asp 67 Replaced By A Gly within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe201 b:50.1 occ:1.00 FE1 E:FES201 0.0 50.1 1.0 S1 E:FES201 2.2 51.7 1.0 S2 E:FES201 2.2 50.1 1.0 SG E:CYS74 2.2 53.7 1.0 SG E:CYS72 2.4 47.8 1.0 FE2 E:FES201 2.8 51.2 1.0 CB E:CYS72 3.4 44.2 1.0 CB E:CYS74 3.4 49.8 1.0 N E:CYS74 3.6 47.8 1.0 CA E:CYS72 3.8 45.4 1.0 CA E:CYS74 4.0 49.1 1.0 N E:ARG73 4.0 46.9 1.0 CB E:HIS87 4.1 55.5 1.0 N E:HIS87 4.2 57.5 1.0 ND1 E:HIS87 4.3 59.4 1.0 C E:CYS72 4.3 50.0 1.0 N E:TRP75 4.3 47.7 1.0 N E:SER77 4.4 50.8 1.0 CB E:SER77 4.4 50.1 1.0 C E:CYS74 4.5 53.6 1.0 CA E:HIS87 4.5 56.7 1.0 N E:ARG76 4.6 47.5 1.0 CG E:HIS87 4.7 58.7 1.0 C E:ARG73 4.7 50.5 1.0 CB E:ALA86 4.9 56.2 1.0 SG E:CYS83 4.9 49.6 1.0 CA E:CYS83 4.9 46.1 1.0 CA E:SER77 4.9 50.9 1.0 C E:ALA86 4.9 63.0 1.0 N E:ALA86 5.0 55.3 1.0 CA E:ARG73 5.0 46.7 1.0

Iron binding site 10 out of 36 in the The Crystal Structure of A Human Mitoneet Mutant with Asp 67 Replaced By A Gly


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of The Crystal Structure of A Human Mitoneet Mutant with Asp 67 Replaced By A Gly within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe201 b:51.2 occ:1.00 FE2 E:FES201 0.0 51.2 1.0 S2 E:FES201 2.2 50.1 1.0 S1 E:FES201 2.2 51.7 1.0 ND1 E:HIS87 2.2 59.4 1.0 SG E:CYS83 2.3 49.6 1.0 FE1 E:FES201 2.8 50.1 1.0 CE1 E:HIS87 3.1 59.6 1.0 CB E:CYS83 3.3 45.5 1.0 CG E:HIS87 3.3 58.7 1.0 CB E:HIS87 3.7 55.5 1.0 CA E:CYS83 3.8 46.1 1.0 N E:GLY85 4.0 52.8 1.0 N E:HIS87 4.1 57.5 1.0 CB E:PRO100 4.2 49.8 1.0 N E:ASP84 4.3 53.0 1.0 NE2 E:HIS87 4.3 61.1 1.0 CA E:GLY85 4.3 53.0 1.0 CD E:PRO100 4.3 50.5 1.0 CD2 E:HIS87 4.4 61.2 1.0 N E:ALA86 4.4 55.3 1.0 C E:CYS83 4.4 55.2 1.0 CG E:PRO100 4.5 54.8 1.0 CA E:CYS72 4.5 45.4 1.0 CA E:HIS87 4.5 56.7 1.0 SG E:CYS74 4.6 53.7 1.0 C E:GLY85 4.6 57.2 1.0 SG E:CYS72 4.6 47.8 1.0 CB E:CYS72 4.6 44.2 1.0 N E:PRO100 4.7 48.8 1.0 CA E:PRO100 4.8 47.7 1.0

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