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Mercury in PDB 1czs: Crystal Structure of the C2 Domain of Human Coagulation Factor V: Complex with Phenylmercury

Protein crystallography data

The structure of Crystal Structure of the C2 Domain of Human Coagulation Factor V: Complex with Phenylmercury, PDB code: 1czs was solved by S.Macedo-Ribeiro, W.Bode, R.Huber, W.H.Kane, P.Fuentes-Prior, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.430, 51.830, 68.150, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 25.8

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of the C2 Domain of Human Coagulation Factor V: Complex with Phenylmercury (pdb code 1czs). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the Crystal Structure of the C2 Domain of Human Coagulation Factor V: Complex with Phenylmercury, PDB code: 1czs:

Mercury binding site 1 out of 1 in 1czs

Go back to Mercury Binding Sites List in 1czs
Mercury binding site 1 out of 1 in the Crystal Structure of the C2 Domain of Human Coagulation Factor V: Complex with Phenylmercury


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structure of the C2 Domain of Human Coagulation Factor V: Complex with Phenylmercury within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg296

b:30.7
occ:0.88
HG A:PHG296 0.0 30.7 0.9
C4 A:PHG296 1.9 34.3 0.0
SG A:CYS76 2.5 25.0 1.0
C3 A:PHG296 2.7 33.2 0.0
O A:HOH216 2.9 12.8 1.0
C5 A:PHG296 3.0 34.6 0.0
NE2 A:GLN48 3.3 23.5 1.0
CB A:CYS76 3.5 20.9 1.0
SD A:MET83 3.6 24.6 1.0
C A:CYS76 3.7 19.5 1.0
O A:CYS76 3.9 18.6 1.0
N A:LYS77 3.9 22.5 1.0
CH2 A:TRP31 4.0 27.1 1.0
CG A:MET83 4.1 24.3 1.0
C2 A:PHG296 4.1 33.3 0.0
CZ3 A:TRP31 4.1 26.0 1.0
CA A:CYS76 4.2 19.2 1.0
C6 A:PHG296 4.3 35.4 0.0
C A:LYS77 4.3 31.1 1.0
CA A:LYS77 4.3 27.0 1.0
CD A:GLN48 4.3 23.7 1.0
O A:LYS77 4.4 34.6 1.0
CB A:MET83 4.6 23.9 1.0
OG1 A:THR148 4.6 33.5 1.0
CE A:MET83 4.6 22.3 1.0
C1 A:PHG296 4.7 34.2 0.0
N A:SER78 4.8 32.6 1.0
CZ2 A:TRP31 4.8 26.0 1.0
CB A:SER78 4.8 34.7 1.0
O A:HOH231 4.9 35.2 1.0
CE3 A:TRP31 4.9 22.6 1.0
N A:CYS76 5.0 17.5 1.0
OD1 A:ASN45 5.0 25.7 1.0
CG A:GLN48 5.0 22.1 1.0

Reference:

S.Macedo-Ribeiro, W.Bode, R.Huber, M.A.Quinn-Allen, S.W.Kim, T.L.Ortel, G.P.Bourenkov, H.D.Bartunik, M.T.Stubbs, W.H.Kane, P.Fuentes-Prior. Crystal Structures of the Membrane-Binding C2 Domain of Human Coagulation Factor V. Nature V. 402 434 1999.
ISSN: ISSN 0028-0836
PubMed: 10586886
DOI: 10.1038/46594
Page generated: Wed Oct 28 18:39:05 2020

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