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Nickel in PDB 3wqa: Acinetobacter Sp. Tol 5 Ataa Ydd-DALL3 Domains in C-Terminal Stalk Fused to GCN4 Adaptors (CSTALKC1II)

Protein crystallography data

The structure of Acinetobacter Sp. Tol 5 Ataa Ydd-DALL3 Domains in C-Terminal Stalk Fused to GCN4 Adaptors (CSTALKC1II), PDB code: 3wqa was solved by K.Koiwai, M.D.Hartmann, S.Yoshimoto, N.Nur 'izzah, A.Suzuki, D.Linke, A.N.Lupas, K.Hori, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.32 / 2.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 86.110, 43.680, 95.564, 90.00, 111.97, 90.00
R / Rfree (%) 21.3 / 30.7

Other elements in 3wqa:

The structure of Acinetobacter Sp. Tol 5 Ataa Ydd-DALL3 Domains in C-Terminal Stalk Fused to GCN4 Adaptors (CSTALKC1II) also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Nickel Binding Sites:

The binding sites of Nickel atom in the Acinetobacter Sp. Tol 5 Ataa Ydd-DALL3 Domains in C-Terminal Stalk Fused to GCN4 Adaptors (CSTALKC1II) (pdb code 3wqa). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Acinetobacter Sp. Tol 5 Ataa Ydd-DALL3 Domains in C-Terminal Stalk Fused to GCN4 Adaptors (CSTALKC1II), PDB code: 3wqa:

Nickel binding site 1 out of 1 in 3wqa

Go back to Nickel Binding Sites List in 3wqa
Nickel binding site 1 out of 1 in the Acinetobacter Sp. Tol 5 Ataa Ydd-DALL3 Domains in C-Terminal Stalk Fused to GCN4 Adaptors (CSTALKC1II)


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Acinetobacter Sp. Tol 5 Ataa Ydd-DALL3 Domains in C-Terminal Stalk Fused to GCN4 Adaptors (CSTALKC1II) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ni3601

b:59.7
occ:1.00
NE2 B:HIS3506 2.2 55.1 1.0
NE2 C:HIS3506 2.3 59.0 1.0
CE1 A:HIS3508 2.4 69.1 1.0
NE2 A:HIS3506 2.7 45.4 1.0
CE1 B:HIS3508 2.8 70.6 1.0
NE2 C:HIS3508 2.8 63.3 1.0
NE2 A:HIS3508 2.9 72.0 1.0
CE1 B:HIS3506 3.0 59.9 1.0
CD2 C:HIS3506 3.1 70.8 1.0
NE2 B:HIS3508 3.2 78.0 1.0
CD2 B:HIS3506 3.3 59.3 1.0
CE1 C:HIS3506 3.4 61.5 1.0
CE1 A:HIS3506 3.5 50.0 1.0
CD2 C:HIS3508 3.5 84.7 1.0
ND1 A:HIS3508 3.5 66.0 1.0
ND1 B:HIS3508 3.6 80.3 1.0
CD2 A:HIS3506 3.6 54.8 1.0
CE1 C:HIS3508 3.8 71.2 1.0
CD2 A:HIS3508 4.1 76.2 1.0
CD2 B:HIS3508 4.1 84.5 1.0
ND1 B:HIS3506 4.2 57.5 1.0
O C:HIS3507 4.2 88.0 1.0
CG C:HIS3506 4.3 72.5 1.0
CG B:HIS3508 4.3 85.4 1.0
CG B:HIS3506 4.3 65.0 1.0
ND1 C:HIS3506 4.4 66.2 1.0
CG A:HIS3508 4.4 69.5 1.0
ND1 A:HIS3506 4.6 49.4 1.0
CG C:HIS3508 4.6 90.1 1.0
CG A:HIS3506 4.7 54.2 1.0
ND1 C:HIS3508 4.8 82.8 1.0
C C:HIS3507 5.0 86.4 1.0

Reference:

K.Koiwai, M.D.Hartmann, S.Yoshimoto, N.Nur 'izzah, D.Linke, A.N.Lupas, K.Hori. Structural Analysis of Acinetobacter Taa-Conserved C-Terminal Domains To Be Published.
Page generated: Wed Oct 9 17:54:07 2024

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