Atomistry » Nickel » PDB 6lv5-6r3z » 6qgr
Atomistry »
  Nickel »
    PDB 6lv5-6r3z »
      6qgr »

Nickel in PDB 6qgr: The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State

Enzymatic activity of The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State

All present enzymatic activity of The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State:
1.12.98.1;

Protein crystallography data

The structure of The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State, PDB code: 6qgr was solved by Y.Ilina, C.Lorent, S.Katz, J.H.Jeoung, S.Shima, M.Horch, I.Zebger, H.Dobbek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.14 / 1.84
Space group F 2 3
Cell size a, b, c (Å), α, β, γ (°) 235.826, 235.826, 235.826, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 22.1

Other elements in 6qgr:

The structure of The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Iron (Fe) 19 atoms

Nickel Binding Sites:

The binding sites of Nickel atom in the The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State (pdb code 6qgr). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State, PDB code: 6qgr:

Nickel binding site 1 out of 1 in 6qgr

Go back to Nickel Binding Sites List in 6qgr
Nickel binding site 1 out of 1 in the The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of The F420-Reducing [Nife] Hydrogenase Complex From Methanosarcina Barkeri at the Nia-S State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni501

b:33.7
occ:1.00
 NI A:NFU501 0.0 33.7 1.0
SG A:CYS63 2.3 31.6 1.0
SG A:CYS432 2.4 38.5 1.0
SG A:CYS66 2.5 33.7 1.0
SG A:CYS435 2.6 35.2 1.0
FE A:NFU501 2.7 32.2 1.0
CB A:CYS63 3.1 29.6 1.0
CB A:CYS432 3.2 31.9 1.0
CB A:CYS66 3.6 31.6 1.0
CB A:CYS435 3.7 30.1 1.0
C1 A:NFU501 3.7 30.1 1.0
C2 A:NFU501 3.8 34.7 1.0
N A:CYS66 3.9 35.5 1.0
CA A:CYS66 4.4 33.1 1.0
C3 A:NFU501 4.4 37.4 1.0
NH2 A:ARG380 4.5 27.0 1.0
CB A:ILE65 4.5 33.0 1.0
CA A:CYS63 4.5 31.3 1.0
N1 A:NFU501 4.6 29.6 1.0
CA A:CYS432 4.7 34.7 1.0
CA A:CYS435 4.7 27.6 1.0
N2 A:NFU501 4.7 28.5 1.0
N A:CYS435 4.7 32.8 1.0
CD A:ARG380 4.7 30.4 1.0
C A:ILE65 4.9 31.7 1.0
N A:ILE65 4.9 30.5 1.0
CZ A:ARG380 5.0 31.3 1.0
C A:CYS63 5.0 34.7 1.0

Reference:

Y.Ilina, C.Lorent, S.Katz, J.H.Jeoung, S.Shima, M.Horch, I.Zebger, H.Dobbek. X-Ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling By [Nife] Hydrogenases. Angew.Chem.Int.Ed.Engl. 2019.
ISSN: ESSN 1521-3773
PubMed: 31591784
DOI: 10.1002/ANIE.201908258
Page generated: Thu Oct 10 08:46:04 2024

Last articles

Zn in 1HYJ
Zn in 1HYT
Zn in 1HYI
Zn in 1HXY
Zn in 1HV5
Zn in 1HWT
Zn in 1HXR
Zn in 1HXP
Zn in 1HXQ
Zn in 1HXK
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy