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Mercury in PDB 1cc8: Crystal Structure of the ATX1 Metallochaperone Protein

Protein crystallography data

The structure of Crystal Structure of the ATX1 Metallochaperone Protein, PDB code: 1cc8 was solved by A.C.Rosenzweig, D.L.Huffman, M.Y.R.A.Pufahl, T.V.O.Hou, A.K.Wernimont, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.02
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 56.650, 29.600, 40.770, 90.00, 114.83, 90.00
R / Rfree (%) 14.6 / 17.2

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of the ATX1 Metallochaperone Protein (pdb code 1cc8). 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 ATX1 Metallochaperone Protein, PDB code: 1cc8:

Mercury binding site 1 out of 1 in 1cc8

Go back to Mercury Binding Sites List in 1cc8
Mercury binding site 1 out of 1 in the Crystal Structure of the ATX1 Metallochaperone Protein


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 ATX1 Metallochaperone Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg74

b:10.6
occ:1.00
SG A:CYS15 2.3 10.2 1.0
SG A:CYS18 2.3 7.8 1.0
OG1 A:THR14 3.1 10.7 1.0
N A:CYS18 3.1 6.4 1.0
N A:CYS15 3.3 8.4 1.0
CB A:CYS18 3.3 6.2 1.0
CB A:CYS15 3.3 10.1 1.0
O A:CYS15 3.5 6.7 1.0
CA A:CYS15 3.6 9.3 1.0
CA A:CYS18 3.7 6.0 1.0
C A:CYS15 3.8 8.1 1.0
C A:GLY17 3.9 7.1 1.0
N A:THR14 4.0 6.3 1.0
C A:THR14 4.0 8.3 1.0
O A:HOH1071 4.1 28.3 1.0
N A:GLY17 4.1 7.5 1.0
O A:HOH1053 4.2 17.1 1.0
CA A:GLY17 4.2 8.1 1.0
CB A:THR14 4.3 8.4 1.0
CA A:THR14 4.3 7.5 1.0
N A:SER16 4.7 8.8 1.0
O A:GLY17 4.9 8.0 1.0
O A:THR14 4.9 10.6 1.0
C A:SER16 5.0 7.8 1.0

Reference:

A.C.Rosenzweig, D.L.Huffman, M.Y.Hou, A.K.Wernimont, R.A.Pufahl, T.V.O'halloran. Crystal Structure of the ATX1 Metallochaperone Protein at 1.02 A Resolution. Structure Fold.Des. V. 7 605 1999.
ISSN: ISSN 0969-2126
PubMed: 10404590
DOI: 10.1016/S0969-2126(99)80082-3
Page generated: Sun Dec 13 19:02:10 2020

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