Atomistry » Mercury » PDB 5lf8-6bvg » 5nm0
Atomistry »
  Mercury »
    PDB 5lf8-6bvg »
      5nm0 »

Mercury in PDB 5nm0: NB36 SER85CYS with Hg, Crystal Form 1

Protein crystallography data

The structure of NB36 SER85CYS with Hg, Crystal Form 1, PDB code: 5nm0 was solved by S.B.Hansen, K.R.Andersen, N.S.Laursen, G.R.Andersen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 71.26 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 37.610, 93.070, 142.510, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 21.1

Mercury Binding Sites:

The binding sites of Mercury atom in the NB36 SER85CYS with Hg, Crystal Form 1 (pdb code 5nm0). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the NB36 SER85CYS with Hg, Crystal Form 1, PDB code: 5nm0:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in 5nm0

Go back to Mercury Binding Sites List in 5nm0
Mercury binding site 1 out of 2 in the NB36 SER85CYS with Hg, Crystal Form 1


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of NB36 SER85CYS with Hg, Crystal Form 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg201

b:39.1
occ:1.00
SG A:CYS85 2.3 27.8 1.0
SG C:CYS85 2.3 22.7 1.0
O C:HOH281 3.0 27.3 1.0
HG2 A:ARG67 3.0 21.5 1.0
HA C:CYS85 3.1 20.1 1.0
O C:HOH217 3.3 24.2 1.0
HB2 A:CYS85 3.3 27.6 1.0
CB C:CYS85 3.3 17.8 1.0
CB A:CYS85 3.3 23.0 1.0
HB3 C:CYS85 3.4 21.3 1.0
HB3 A:CYS85 3.5 27.6 1.0
HA A:ARG67 3.5 23.1 1.0
CA C:CYS85 3.6 16.8 1.0
H C:CYS85 3.8 20.1 1.0
O A:GLY66 4.0 26.3 1.0
CG A:ARG67 4.0 17.9 1.0
O C:GLY16 4.0 25.5 1.0
N C:CYS85 4.0 16.7 1.0
HB2 C:CYS85 4.2 21.3 1.0
O C:HOH282 4.3 47.5 1.0
CA A:ARG67 4.3 19.2 1.0
HB3 A:ARG67 4.3 24.4 1.0
CB A:ARG67 4.4 20.3 1.0
HA2 C:GLY16 4.4 30.5 1.0
O A:HOH360 4.5 37.7 1.0
HD2 A:ARG67 4.5 26.8 1.0
C A:GLY66 4.6 23.8 1.0
HD3 A:ARG67 4.6 26.8 1.0
HG3 A:ARG67 4.6 21.5 1.0
HB3 C:ASN84 4.6 21.0 1.0
CD A:ARG67 4.6 22.3 1.0
HB2 A:ASN84 4.7 28.1 1.0
O A:HOH345 4.7 39.4 1.0
N A:ARG67 4.7 20.9 1.0
CA A:CYS85 4.8 24.4 1.0
HB3 A:ASN84 4.9 28.1 1.0
C C:GLY16 4.9 23.7 1.0
C C:CYS85 5.0 20.3 1.0

Mercury binding site 2 out of 2 in 5nm0

Go back to Mercury Binding Sites List in 5nm0
Mercury binding site 2 out of 2 in the NB36 SER85CYS with Hg, Crystal Form 1


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of NB36 SER85CYS with Hg, Crystal Form 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg201

b:37.9
occ:1.00
SG B:CYS85 2.3 26.6 1.0
SG D:CYS85 2.3 26.0 1.0
O D:HOH266 2.9 34.3 1.0
HG D:CYS85 3.0 31.2 1.0
HA D:CYS85 3.1 27.3 1.0
HG2 B:ARG67 3.1 24.3 1.0
HB2 B:CYS85 3.3 34.0 1.0
CB B:CYS85 3.3 28.4 1.0
CB D:CYS85 3.4 21.2 1.0
O D:HOH219 3.4 24.8 1.0
HB3 D:CYS85 3.5 25.4 1.0
HB3 B:CYS85 3.5 34.0 1.0
HA B:ARG67 3.6 24.4 1.0
CA D:CYS85 3.6 22.8 1.0
H D:CYS85 3.8 26.0 1.0
O B:GLY66 3.9 26.3 1.0
N D:CYS85 4.0 21.7 1.0
CG B:ARG67 4.1 20.2 1.0
O D:GLY16 4.1 33.5 1.0
HB2 D:CYS85 4.2 25.4 1.0
CA B:ARG67 4.4 20.3 1.0
HB3 B:ARG67 4.4 27.1 1.0
HA2 D:GLY16 4.5 37.2 1.0
CB B:ARG67 4.5 22.6 1.0
HD2 B:ARG67 4.5 25.7 1.0
C B:GLY66 4.6 21.9 1.0
O B:HOH348 4.6 41.0 1.0
HD3 B:ARG67 4.6 25.7 1.0
HB3 D:ASN84 4.6 23.7 1.0
HG3 B:ARG67 4.7 24.3 1.0
CD B:ARG67 4.7 21.4 1.0
CA B:CYS85 4.7 23.4 1.0
N B:ARG67 4.8 20.5 1.0
O B:HOH368 4.8 37.0 1.0
HB2 B:ASN84 4.8 27.1 1.0

Reference:

S.B.Hansen, N.S.Laursen, G.R.Andersen, K.R.Andersen. Introducing Site-Specific Cysteines Into Nanobodies For Mercury Labelling Allows De Novo Phasing of Their Crystal Structures. Acta Crystallogr D Struct V. 73 804 2017BIOL.
ISSN: ISSN 2059-7983
PubMed: 28994409
DOI: 10.1107/S2059798317013171
Page generated: Sun Dec 13 19:13:03 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