Iron in PDB 6vxt: Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii

Enzymatic activity of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii

All present enzymatic activity of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii:
1.18.6.1;

Protein crystallography data

The structure of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii, PDB code: 6vxt was solved by W.Kang, Y.Hu, M.W.Ribbe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.71 / 1.74
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 163.535, 203.435, 83.857, 90.00, 103.95, 90.00
R / Rfree (%) 17.2 / 20.3

Other elements in 6vxt:

The structure of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii also contains other interesting chemical elements:

Molybdenum (Mo) 10 atoms

Iron Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 32;

Binding sites:

The binding sites of Iron atom in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii (pdb code 6vxt). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 32 binding sites of Iron where determined in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii, PDB code: 6vxt:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 32 in 6vxt

Go back to Iron Binding Sites List in 6vxt
Iron binding site 1 out of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe602

b:33.8
occ:1.00
FE1 A:ICS602 0.0 33.8 1.0
S2A A:ICS602 2.3 28.6 1.0
S4A A:ICS602 2.3 31.4 1.0
S1A A:ICS602 2.3 30.6 1.0
SG A:CYS275 2.4 35.5 1.0
FE3 A:ICS602 2.6 31.5 1.0
FE2 A:ICS602 2.6 32.2 1.0
FE4 A:ICS602 2.7 31.4 1.0
CB A:CYS275 3.3 30.2 1.0
CX A:ICS602 3.4 27.1 1.0
OG A:SER278 4.0 32.1 1.0
CB A:LEU358 4.1 34.8 1.0
CB A:SER278 4.4 34.1 1.0
CA A:CYS275 4.5 33.8 1.0
CE2 A:TYR229 4.6 33.0 1.0
CD2 A:LEU358 4.7 36.3 1.0
S5A A:ICS602 4.8 28.7 1.0
S2B A:ICS602 4.8 31.9 1.0
S3A A:ICS602 4.8 30.8 1.0
N A:SER278 5.0 36.4 1.0
FE6 A:ICS602 5.0 30.5 1.0
FE5 A:ICS602 5.0 30.8 1.0
N A:LEU358 5.0 33.5 1.0
CD2 A:TYR229 5.0 33.3 1.0
FE7 A:ICS602 5.0 31.6 1.0

Iron binding site 2 out of 32 in 6vxt

Go back to Iron Binding Sites List in 6vxt
Iron binding site 2 out of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe602

b:32.2
occ:1.00
FE2 A:ICS602 0.0 32.2 1.0
CX A:ICS602 2.0 27.1 1.0
S2A A:ICS602 2.2 28.6 1.0
S2B A:ICS602 2.2 31.9 1.0
S1A A:ICS602 2.3 30.6 1.0
FE6 A:ICS602 2.6 30.5 1.0
FE4 A:ICS602 2.6 31.4 1.0
FE1 A:ICS602 2.6 33.8 1.0
FE3 A:ICS602 2.7 31.5 1.0
FE5 A:ICS602 3.6 30.8 1.0
FE7 A:ICS602 3.7 31.6 1.0
S4A A:ICS602 3.8 31.4 1.0
NE2 A:HIS195 4.1 35.8 1.0
CZ A:PHE381 4.1 33.0 1.0
S1B A:ICS602 4.2 27.2 1.0
S3B A:ICS602 4.2 31.0 1.0
CE1 A:HIS195 4.2 36.4 1.0
S3A A:ICS602 4.4 30.8 1.0
S5A A:ICS602 4.5 28.7 1.0
CE1 A:PHE381 4.5 31.6 1.0
CG1 A:VAL70 4.6 34.2 1.0
SG A:CYS275 4.7 35.5 1.0
N A:GLY357 4.9 35.7 1.0

Iron binding site 3 out of 32 in 6vxt

Go back to Iron Binding Sites List in 6vxt
Iron binding site 3 out of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe602

b:31.5
occ:1.00
FE3 A:ICS602 0.0 31.5 1.0
CX A:ICS602 2.0 27.1 1.0
S5A A:ICS602 2.2 28.7 1.0
S4A A:ICS602 2.2 31.4 1.0
S2A A:ICS602 2.3 28.6 1.0
FE1 A:ICS602 2.6 33.8 1.0
FE2 A:ICS602 2.7 32.2 1.0
FE4 A:ICS602 2.7 31.4 1.0
FE7 A:ICS602 2.7 31.6 1.0
FE6 A:ICS602 3.7 30.5 1.0
FE5 A:ICS602 3.8 30.8 1.0
S1A A:ICS602 3.8 30.6 1.0
NH2 A:ARG96 4.1 31.2 1.0
O A:HOH906 4.1 34.8 1.0
CD2 A:TYR229 4.2 33.3 1.0
S3B A:ICS602 4.3 31.0 1.0
S4B A:ICS602 4.3 29.4 1.0
CE2 A:TYR229 4.5 33.0 1.0
S2B A:ICS602 4.5 31.9 1.0
S3A A:ICS602 4.6 30.8 1.0
SG A:CYS275 4.9 35.5 1.0

Iron binding site 4 out of 32 in 6vxt

Go back to Iron Binding Sites List in 6vxt
Iron binding site 4 out of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe602

b:31.4
occ:1.00
FE4 A:ICS602 0.0 31.4 1.0
CX A:ICS602 2.0 27.1 1.0
S3A A:ICS602 2.2 30.8 1.0
S4A A:ICS602 2.3 31.4 1.0
S1A A:ICS602 2.3 30.6 1.0
FE5 A:ICS602 2.6 30.8 1.0
FE2 A:ICS602 2.6 32.2 1.0
FE1 A:ICS602 2.7 33.8 1.0
FE3 A:ICS602 2.7 31.5 1.0
FE6 A:ICS602 3.7 30.5 1.0
FE7 A:ICS602 3.7 31.6 1.0
S2A A:ICS602 3.8 28.6 1.0
N A:GLY357 4.0 35.7 1.0
N A:LEU358 4.0 33.5 1.0
CB A:LEU358 4.0 34.8 1.0
S4B A:ICS602 4.2 29.4 1.0
S1B A:ICS602 4.3 27.2 1.0
S5A A:ICS602 4.4 28.7 1.0
S2B A:ICS602 4.5 31.9 1.0
N A:ARG359 4.5 31.6 1.0
CA A:LEU358 4.6 32.9 1.0
C A:GLY357 4.6 38.2 1.0
CG A:ARG359 4.6 29.7 1.0
CA A:GLY357 4.6 31.7 1.0
SG A:CYS275 4.7 35.5 1.0
CD A:ARG359 4.8 31.5 1.0
CA A:GLY356 4.8 35.0 1.0
C A:GLY356 4.9 36.0 1.0
NE A:ARG359 4.9 33.0 1.0

Iron binding site 5 out of 32 in 6vxt

Go back to Iron Binding Sites List in 6vxt
Iron binding site 5 out of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe602

b:30.8
occ:1.00
FE5 A:ICS602 0.0 30.8 1.0
CX A:ICS602 2.0 27.1 1.0
S1B A:ICS602 2.2 27.2 1.0
S4B A:ICS602 2.2 29.4 1.0
S3A A:ICS602 2.3 30.8 1.0
FE6 A:ICS602 2.6 30.5 1.0
FE4 A:ICS602 2.6 31.4 1.0
FE7 A:ICS602 2.6 31.6 1.0
MO1 A:ICS602 2.7 32.2 1.0
FE2 A:ICS602 3.6 32.2 1.0
FE3 A:ICS602 3.8 31.5 1.0
ND1 A:HIS442 3.8 28.2 1.0
S3B A:ICS602 3.8 31.0 1.0
N A:GLY356 4.1 32.8 1.0
CA A:GLY356 4.1 35.0 1.0
CE1 A:HIS442 4.2 33.4 1.0
CG2 A:ILE355 4.2 30.5 1.0
S1A A:ICS602 4.3 30.6 1.0
S4A A:ICS602 4.3 31.4 1.0
S2B A:ICS602 4.4 31.9 1.0
S5A A:ICS602 4.4 28.7 1.0
N A:GLY357 4.6 35.7 1.0
CD A:ARG359 4.7 31.5 1.0
O6 A:HCA601 4.7 24.4 1.0
O7 A:HCA601 4.8 35.8 1.0
CG A:HIS442 4.8 31.8 1.0
C A:GLY356 4.9 36.0 1.0
FE1 A:ICS602 5.0 33.8 1.0

Iron binding site 6 out of 32 in 6vxt

Go back to Iron Binding Sites List in 6vxt
Iron binding site 6 out of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe602

b:30.5
occ:1.00
FE6 A:ICS602 0.0 30.5 1.0
CX A:ICS602 2.0 27.1 1.0
S1B A:ICS602 2.2 27.2 1.0
S2B A:ICS602 2.2 31.9 1.0
S3B A:ICS602 2.2 31.0 1.0
FE5 A:ICS602 2.6 30.8 1.0
FE7 A:ICS602 2.6 31.6 1.0
FE2 A:ICS602 2.6 32.2 1.0
MO1 A:ICS602 2.6 32.2 1.0
FE4 A:ICS602 3.7 31.4 1.0
FE3 A:ICS602 3.7 31.5 1.0
S4B A:ICS602 3.8 29.4 1.0
O7 A:HCA601 3.8 35.8 1.0
CZ A:PHE381 4.1 33.0 1.0
S2A A:ICS602 4.2 28.6 1.0
S1A A:ICS602 4.3 30.6 1.0
S5A A:ICS602 4.4 28.7 1.0
S3A A:ICS602 4.5 30.8 1.0
O6 A:HCA601 4.5 24.4 1.0
CG2 A:VAL70 4.5 29.2 1.0
O2 A:HCA601 4.6 31.1 1.0
ND1 A:HIS442 4.7 28.2 1.0
CE2 A:PHE381 4.7 32.5 1.0
C3 A:HCA601 4.8 36.5 1.0
FE1 A:ICS602 5.0 33.8 1.0
C2 A:HCA601 5.0 32.7 1.0

Iron binding site 7 out of 32 in 6vxt

Go back to Iron Binding Sites List in 6vxt
Iron binding site 7 out of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe602

b:31.6
occ:1.00
FE7 A:ICS602 0.0 31.6 1.0
CX A:ICS602 2.0 27.1 1.0
S5A A:ICS602 2.2 28.7 1.0
S4B A:ICS602 2.2 29.4 1.0
S3B A:ICS602 2.2 31.0 1.0
FE6 A:ICS602 2.6 30.5 1.0
FE5 A:ICS602 2.6 30.8 1.0
MO1 A:ICS602 2.6 32.2 1.0
FE3 A:ICS602 2.7 31.5 1.0
FE4 A:ICS602 3.7 31.4 1.0
FE2 A:ICS602 3.7 32.2 1.0
O6 A:HCA601 3.7 24.4 1.0
S1B A:ICS602 3.8 27.2 1.0
O A:HOH876 3.8 32.6 1.0
NE A:ARG96 4.2 32.0 1.0
S2A A:ICS602 4.3 28.6 1.0
NH2 A:ARG96 4.3 31.2 1.0
S4A A:ICS602 4.3 31.4 1.0
S2B A:ICS602 4.4 31.9 1.0
S3A A:ICS602 4.5 30.8 1.0
C7 A:HCA601 4.7 31.8 1.0
ND1 A:HIS442 4.7 28.2 1.0
O7 A:HCA601 4.7 35.8 1.0
CZ A:ARG96 4.8 31.9 1.0
CZ A:ARG359 4.8 32.9 1.0
NH1 A:ARG359 4.8 32.3 1.0
FE1 A:ICS602 5.0 33.8 1.0

Iron binding site 8 out of 32 in 6vxt

Go back to Iron Binding Sites List in 6vxt
Iron binding site 8 out of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe608

b:33.0
occ:1.00
FE1 A:CLF608 0.0 33.0 1.0
S3A A:CLF608 2.3 32.0 1.0
S2A A:CLF608 2.3 34.2 1.0
S1 A:CLF608 2.4 32.6 1.0
SG A:CYS154 2.4 32.4 1.0
FE2 A:CLF608 2.5 32.9 1.0
FE4 A:CLF608 2.5 32.5 1.0
FE3 A:CLF608 2.7 32.0 1.0
CB A:CYS154 3.3 34.4 1.0
S4A A:CLF608 3.8 32.2 1.0
O B:HOH739 3.8 33.4 1.0
N A:CYS154 3.9 34.6 1.0
CA A:GLY185 3.9 35.9 1.0
OG B:SER92 4.0 34.3 0.5
N A:GLY185 4.1 37.1 1.0
CA A:CYS154 4.2 31.1 1.0
SG B:CYS95 4.2 32.3 1.0
FE8 A:CLF608 4.4 33.5 1.0
FE5 A:CLF608 4.5 32.5 1.0
SG A:CYS88 4.6 35.1 1.0
C A:GLY185 4.7 36.5 1.0
CB B:SER92 4.8 42.0 1.0
FE6 A:CLF608 4.8 35.5 1.0
SG A:CYS62 4.9 31.7 1.0
SG B:CYS153 5.0 35.3 1.0

Iron binding site 9 out of 32 in 6vxt

Go back to Iron Binding Sites List in 6vxt
Iron binding site 9 out of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe608

b:32.9
occ:1.00
FE2 A:CLF608 0.0 32.9 1.0
S2A A:CLF608 2.3 34.2 1.0
S4A A:CLF608 2.3 32.2 1.0
SG B:CYS95 2.4 32.3 1.0
FE1 A:CLF608 2.5 33.0 1.0
S1 A:CLF608 2.5 32.6 1.0
FE4 A:CLF608 2.5 32.5 1.0
FE3 A:CLF608 2.7 32.0 1.0
FE8 A:CLF608 3.0 33.5 1.0
N B:CYS95 3.3 37.9 1.0
CA B:CYS95 3.6 28.8 1.0
CB B:CYS95 3.6 26.3 1.0
FE5 A:CLF608 3.7 32.5 1.0
S3A A:CLF608 3.8 32.0 1.0
C B:GLY94 3.9 33.3 1.0
S4B A:CLF608 3.9 29.1 1.0
OG B:SER92 4.2 34.3 0.5
CA B:GLY94 4.4 32.4 1.0
O B:HOH739 4.4 33.4 1.0
SG A:CYS88 4.6 35.1 1.0
FE6 A:CLF608 4.6 35.5 1.0
SG A:CYS154 4.6 32.4 1.0
O B:GLY94 4.6 32.8 1.0
SG A:CYS62 4.8 31.7 1.0
N B:GLY94 4.8 32.5 1.0

Iron binding site 10 out of 32 in 6vxt

Go back to Iron Binding Sites List in 6vxt
Iron binding site 10 out of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe608

b:32.0
occ:1.00
FE3 A:CLF608 0.0 32.0 1.0
S4A A:CLF608 2.3 32.2 1.0
S2A A:CLF608 2.3 34.2 1.0
S3A A:CLF608 2.3 32.0 1.0
SG A:CYS62 2.4 31.7 1.0
FE4 A:CLF608 2.6 32.5 1.0
FE2 A:CLF608 2.7 32.9 1.0
FE1 A:CLF608 2.7 33.0 1.0
CB A:CYS62 3.4 31.1 1.0
CA A:GLY185 3.9 35.9 1.0
CB A:TYR64 4.1 28.6 1.0
S1 A:CLF608 4.2 32.6 1.0
CA B:GLY94 4.2 32.4 1.0
C B:GLY94 4.5 33.3 1.0
N A:GLY185 4.5 37.1 1.0
CD1 A:TYR64 4.6 36.0 1.0
CG A:TYR64 4.6 33.6 1.0
N B:CYS95 4.6 37.9 1.0
SG A:CYS154 4.8 32.4 1.0
CA A:CYS62 4.8 30.2 1.0
O B:HOH970 4.8 34.3 1.0
SG A:CYS88 4.9 35.1 1.0
N A:TYR64 4.9 34.4 1.0
N B:GLY94 5.0 32.5 1.0
CE2 B:TYR98 5.0 34.2 1.0
C A:GLY185 5.0 36.5 1.0

Reference:

W.Kang, C.C.Lee, A.J.Jasniewski, M.W.Ribbe, Y.Hu. Structural Evidence For A Dynamic Metallocofactor During N Reduction By Mo-Nitrogenase Science 2020.
ISSN: ESSN 1095-9203
DOI: 10.1126/SCIENCE.AAZ6748
Page generated: Sun Dec 13 17:23:31 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy