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Mercury in PDB 4ihd: Crystal Structure of Uncleaved Thnt T282C, Derivatized at the Active Site with Ethg

Enzymatic activity of Crystal Structure of Uncleaved Thnt T282C, Derivatized at the Active Site with Ethg

All present enzymatic activity of Crystal Structure of Uncleaved Thnt T282C, Derivatized at the Active Site with Ethg:
3.5.1.92;

Protein crystallography data

The structure of Crystal Structure of Uncleaved Thnt T282C, Derivatized at the Active Site with Ethg, PDB code: 4ihd was solved by A.R.Buller, J.F.Schildbach, C.A.Townsend, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.70 / 1.65
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 140.611, 68.950, 73.827, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 18.5

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of Uncleaved Thnt T282C, Derivatized at the Active Site with Ethg (pdb code 4ihd). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Crystal Structure of Uncleaved Thnt T282C, Derivatized at the Active Site with Ethg, PDB code: 4ihd:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in 4ihd

Go back to Mercury Binding Sites List in 4ihd
Mercury binding site 1 out of 2 in the Crystal Structure of Uncleaved Thnt T282C, Derivatized at the Active Site with Ethg


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 Uncleaved Thnt T282C, Derivatized at the Active Site with Ethg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg401

b:31.2
occ:0.45
HG A:EMC401 0.0 31.2 0.5
CB A:CYS282 2.0 19.8 0.3
C1 A:EMC401 2.4 31.0 0.5
O A:HOH867 2.5 31.0 1.0
SG A:CYS282 2.5 24.4 0.7
SG A:CYS282 2.7 20.0 0.3
O A:ALA142 2.7 21.4 1.0
O A:GLY322 2.8 29.5 1.0
CA A:CYS282 2.9 19.9 0.3
CB A:CYS282 3.0 23.2 0.7
C2 A:EMC401 3.3 30.6 0.5
CD2 A:LEU284 3.4 20.5 1.0
C A:CYS282 3.4 19.5 0.3
C A:GLY322 3.7 27.0 1.0
C A:ALA142 3.8 19.2 1.0
O A:CYS282 3.9 18.6 0.3
CA A:GLY322 4.0 28.1 1.0
N A:THR283 4.0 19.1 0.3
CA A:LEU143 4.1 17.8 1.0
N A:CYS282 4.2 20.9 0.3
O A:HOH786 4.2 14.4 0.4
N A:LEU143 4.4 18.1 1.0
CG A:LEU284 4.4 20.4 1.0
O A:ASN281 4.4 21.8 0.3
CA A:CYS282 4.5 22.8 0.7
N A:GLY322 4.6 28.1 1.0
CB A:LEU143 4.6 17.9 1.0
O A:HOH866 4.7 38.1 1.0
O A:HOH843 4.7 29.9 1.0
C A:ASN281 4.7 22.2 0.3
N A:ALA142 4.8 17.6 1.0
N A:ASP323 4.8 25.8 1.0
O A:ASN281 4.8 24.4 0.7
O A:THR283 4.8 19.4 0.3
CD1 A:LEU284 4.9 21.5 1.0
CA A:ALA142 5.0 17.9 1.0

Mercury binding site 2 out of 2 in 4ihd

Go back to Mercury Binding Sites List in 4ihd
Mercury binding site 2 out of 2 in the Crystal Structure of Uncleaved Thnt T282C, Derivatized at the Active Site with Ethg


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Crystal Structure of Uncleaved Thnt T282C, Derivatized at the Active Site with Ethg within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg401

b:35.5
occ:0.45
HG B:EMC401 0.0 35.5 0.5
C1 B:EMC401 2.4 34.6 0.5
O B:HOH776 2.4 41.5 1.0
SG B:CYS282 2.6 35.0 1.0
O B:ALA142 2.7 25.1 1.0
O B:HOH783 2.8 33.0 0.6
O B:GLY322 2.9 29.8 1.0
CB B:CYS282 3.0 31.5 1.0
C2 B:EMC401 3.3 34.4 0.5
CD2 B:LEU284 3.3 25.7 1.0
C B:GLY322 3.6 28.4 1.0
C B:ALA142 3.8 23.6 1.0
CA B:GLY322 3.9 29.8 1.0
CA B:LEU143 4.2 23.0 1.0
O B:HOH566 4.3 28.9 1.0
CG B:LEU284 4.4 24.9 1.0
N B:LEU143 4.4 23.2 1.0
N B:GLY322 4.5 30.1 1.0
CA B:CYS282 4.5 30.9 1.0
CB B:LEU143 4.7 23.0 1.0
O B:HOH775 4.8 41.2 1.0
N B:ALA142 4.8 21.7 1.0
N B:ASP323 4.8 27.7 1.0
O B:ASN281 4.8 32.4 1.0
O B:HOH583 4.8 35.2 1.0
CD1 B:LEU284 4.9 25.9 1.0
CA B:ALA142 5.0 22.6 1.0
OG1 B:THR324 5.0 28.3 1.0

Reference:

A.R.Buller, M.F.Freeman, J.F.Schildbach, C.A.Townsend. Exploring the Role of Conformational Heterogeneity in Cis-Autoproteolytic Activation of Thnt. Biochemistry V. 53 4273 2014.
ISSN: ISSN 0006-2960
PubMed: 24933323
DOI: 10.1021/BI500385D
Page generated: Sun Aug 11 04:53:48 2024

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