Atomistry » Molybdenum » PDB 6op4-8ccq » 7ut6
Atomistry »
  Molybdenum »
    PDB 6op4-8ccq »
      7ut6 »

Molybdenum in PDB 7ut6: C1 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions

Enzymatic activity of C1 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions

All present enzymatic activity of C1 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions:
1.18.6.1;

Other elements in 7ut6:

The structure of C1 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions also contains other interesting chemical elements:

Iron (Fe) 32 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the C1 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions (pdb code 7ut6). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the C1 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions, PDB code: 7ut6:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 7ut6

Go back to Molybdenum Binding Sites List in 7ut6
Molybdenum binding site 1 out of 2 in the C1 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of C1 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo502

b:38.4
occ:1.00
MO1 A:ICS502 0.0 38.4 1.0
S1B A:ICS502 2.3 28.9 1.0
S4B A:ICS502 2.3 23.7 1.0
S3B A:ICS502 2.4 26.0 1.0
O6 A:HCA501 2.6 14.7 1.0
ND1 A:HIS442 2.7 27.3 1.0
FE6 A:ICS502 2.7 30.3 1.0
FE7 A:ICS502 2.7 35.2 1.0
FE5 A:ICS502 2.7 27.0 1.0
O7 A:HCA501 2.7 25.5 1.0
C7 A:HCA501 3.5 21.9 1.0
CX A:ICS502 3.5 19.8 1.0
CG A:HIS442 3.6 23.5 1.0
CE1 A:HIS442 3.6 17.6 1.0
C3 A:HCA501 3.7 19.6 1.0
CB A:HIS442 3.7 22.4 1.0
O2 A:HCA501 4.2 32.5 1.0
O A:HOH619 4.3 22.5 1.0
C5 A:HCA501 4.4 20.3 1.0
CA A:HIS442 4.5 22.0 1.0
O5 A:HCA501 4.6 31.9 1.0
C2 A:HCA501 4.6 23.9 1.0
C4 A:HCA501 4.7 27.1 1.0
NE2 A:HIS442 4.7 23.7 1.0
CD2 A:HIS442 4.7 16.4 1.0
S2B A:ICS502 4.8 23.7 1.0
S5A A:ICS502 4.8 26.8 1.0
S3A A:ICS502 4.9 30.0 1.0
C1 A:HCA501 4.9 25.8 1.0

Molybdenum binding site 2 out of 2 in 7ut6

Go back to Molybdenum Binding Sites List in 7ut6
Molybdenum binding site 2 out of 2 in the C1 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of C1 Symmetric Cryoem Structure of Azotobacter Vinelandii Mofep Under Non-Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mo502

b:35.4
occ:1.00
MO1 C:ICS502 0.0 35.4 1.0
S1B C:ICS502 2.3 25.7 1.0
S4B C:ICS502 2.3 19.8 1.0
S3B C:ICS502 2.4 24.6 1.0
O6 C:HCA501 2.6 10.6 1.0
ND1 C:HIS442 2.6 23.0 1.0
FE6 C:ICS502 2.7 27.3 1.0
FE7 C:ICS502 2.7 35.0 1.0
FE5 C:ICS502 2.7 28.2 1.0
O7 C:HCA501 2.7 21.5 1.0
C7 C:HCA501 3.4 20.0 1.0
CX C:ICS502 3.5 20.8 1.0
CE1 C:HIS442 3.6 15.3 1.0
CG C:HIS442 3.6 18.9 1.0
C3 C:HCA501 3.6 17.2 1.0
CB C:HIS442 3.8 20.2 1.0
O2 C:HCA501 4.2 28.8 1.0
C5 C:HCA501 4.3 17.4 1.0
O C:HOH624 4.4 19.5 1.0
CA C:HIS442 4.5 17.0 1.0
O5 C:HCA501 4.6 28.9 1.0
C2 C:HCA501 4.6 18.4 1.0
C4 C:HCA501 4.6 20.3 1.0
NE2 C:HIS442 4.7 19.6 1.0
CD2 C:HIS442 4.7 15.5 1.0
S2B C:ICS502 4.8 22.2 1.0
S5A C:ICS502 4.8 23.5 1.0
C1 C:HCA501 4.9 20.9 1.0
S3A C:ICS502 4.9 26.6 1.0

Reference:

H.L.Rutledge, B.D.Cook, H.P.M.Nguyen, M.A.Herzik Jr., F.A.Tezcan. Structures of the Nitrogenase Complex Prepared Under Catalytic Turnover Conditions. Science V. 377 865 2022.
ISSN: ESSN 1095-9203
PubMed: 35901182
DOI: 10.1126/SCIENCE.ABQ7641
Page generated: Sun Oct 6 17:01:03 2024

Last articles

W in 8QLN
W in 8RJA
V in 8WTN
Te in 8QLN
Re in 9GHX
Rb in 8Z5C
Ni in 9C0T
Ni in 9C0S
Ni in 9GP1
Ni in 9FYO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy