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Mercury in PDB 7qld: Crystal Structure of S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198)

Protein crystallography data

The structure of Crystal Structure of S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198), PDB code: 7qld was solved by T.Sagmeister, D.Vejzovic, M.Eder, A.Dordic, T.Pavkov-Keller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.38 / 2.15
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 85.36, 85.36, 191.965, 90, 90, 120
R / Rfree (%) 21.9 / 26.6

Other elements in 7qld:

The structure of Crystal Structure of S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198) also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198) (pdb code 7qld). 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 S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198), PDB code: 7qld:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in 7qld

Go back to Mercury Binding Sites List in 7qld
Mercury binding site 1 out of 2 in the Crystal Structure of S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198)


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 S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg201

b:73.7
occ:0.39
SG B:CYS146 2.5 75.8 1.0
CL B:CL202 2.5 64.6 1.0
CL B:CL203 2.6 75.1 1.0
HG21 B:THR55 2.8 47.3 1.0
O B:VAL54 3.0 48.3 1.0
HG B:CYS146 3.0 70.8 1.0
HA B:THR55 3.1 51.0 1.0
H B:ASN148 3.1 66.8 1.0
HA B:CYS146 3.4 65.6 1.0
HB3 B:ASN148 3.5 61.6 1.0
H B:ALA147 3.5 67.1 1.0
CG2 B:THR55 3.7 46.4 1.0
HB2 B:ASN148 3.7 61.6 1.0
HG23 B:THR55 3.8 47.2 1.0
CB B:CYS146 3.8 62.5 1.0
HD3 B:PRO56 3.9 49.1 1.0
CA B:CYS146 4.0 66.0 1.0
C B:VAL54 4.0 50.0 1.0
N B:ALA147 4.0 65.9 1.0
CA B:THR55 4.0 52.5 1.0
N B:ASN148 4.0 67.6 1.0
HD2 B:PRO56 4.0 49.1 1.0
CB B:ASN148 4.0 61.0 1.0
HB2 B:CYS146 4.2 66.2 1.0
HG22 B:VAL151 4.3 53.8 1.0
OD1 B:ASP53 4.3 83.5 1.0
C B:CYS146 4.3 70.8 1.0
HB3 B:ALA147 4.3 67.5 1.0
HG22 B:THR55 4.4 47.2 1.0
CB B:THR55 4.4 49.1 1.0
CD B:PRO56 4.4 49.2 1.0
N B:THR55 4.4 51.5 1.0
HB3 B:CYS146 4.6 66.2 1.0
HB B:THR55 4.6 49.1 1.0
CA B:ASN148 4.7 62.3 1.0
HD22 B:ASN148 4.8 68.1 1.0
CA B:ALA147 4.9 66.5 1.0
C B:ALA147 4.9 69.6 1.0

Mercury binding site 2 out of 2 in 7qld

Go back to Mercury Binding Sites List in 7qld
Mercury binding site 2 out of 2 in the Crystal Structure of S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198)


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 S-Layer Protein Slpa From Lactobacillus Acidophilus, Domain I, Co-Crystallization with HGCL2, Mutation SER146CYS, (Aa 32-198) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg201

b:97.2
occ:0.44
SG A:CYS146 2.6 143.0 1.0
CL A:CL202 2.7 103.7 1.0
CL A:CL203 2.7 79.2 0.7
O A:CYS146 2.9 85.2 1.0
O A:VAL151 3.1 68.2 1.0
HG A:CYS146 3.4 123.2 1.0
O A:ASN148 3.4 90.0 1.0
HB3 A:CYS146 3.4 104.6 1.0
HB A:VAL151 3.4 69.7 1.0
O A:SER167 3.5 73.7 1.0
H A:CYS146 3.5 77.2 1.0
CB A:CYS146 3.5 96.7 1.0
HA A:SER167 3.6 75.7 1.0
C A:CYS146 3.7 99.0 1.0
N A:CYS146 3.8 73.5 1.0
HA A:SER149 3.8 77.5 1.0
CA A:CYS146 3.8 91.8 1.0
HB3 A:SER167 3.8 85.1 1.0
H A:VAL151 4.0 68.7 1.0
C A:VAL151 4.1 64.0 1.0
HG11 A:VAL151 4.2 67.4 1.0
CA A:SER167 4.2 80.4 1.0
C A:ASN148 4.3 87.1 1.0
C A:SER167 4.3 69.4 1.0
CB A:VAL151 4.3 69.8 1.0
HZ1 A:LYS152 4.3 93.6 1.0
HB2 A:CYS146 4.4 104.7 1.0
CB A:SER167 4.4 81.9 1.0
HE2 A:PHE153 4.4 65.1 1.0
CA A:VAL151 4.6 69.7 1.0
CA A:SER149 4.6 79.9 1.0
C A:GLY145 4.7 72.2 1.0
HA2 A:GLY145 4.7 73.1 1.0
N A:VAL151 4.7 69.1 1.0
HA A:LYS152 4.7 68.5 1.0
HD3 A:LYS152 4.7 82.2 1.0
OG A:SER167 4.7 98.2 1.0
CG1 A:VAL151 4.7 66.3 1.0
HA A:CYS146 4.8 90.1 1.0
N A:SER149 4.8 86.7 1.0
N A:ALA147 4.9 92.2 1.0
H A:ASN148 5.0 84.5 1.0
N A:ASN148 5.0 83.3 1.0

Reference:

T.Sagmeister, M.Eder, C.Grininger, D.Vejzovic, C.Buhlheller, A.Dordic, E.Damisch, C.Millan, A.Medina, I.Uson, M.Baek, R.Read, D.Baker, T.Pavkov-Keller. The Self-Assembly of the S-Layer Protein From Lactobacilli Acidophilus To Be Published.
Page generated: Sun Aug 11 08:40:00 2024

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