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Nickel in PDB 6yoa: Lig V 1 Structure and the Inflammatory Response to the Ole E 1 Protein Family

Protein crystallography data

The structure of Lig V 1 Structure and the Inflammatory Response to the Ole E 1 Protein Family, PDB code: 6yoa was solved by T.Robledo-Retana, J.Bradley-Clark, T.Croll, R.Rose, A.Stagg, M.Villalba, R.Pickersgill, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.10 / 2.83
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 76.484, 76.484, 113.498, 90.00, 90.00, 120.00
R / Rfree (%) 26.2 / 31.9

Nickel Binding Sites:

The binding sites of Nickel atom in the Lig V 1 Structure and the Inflammatory Response to the Ole E 1 Protein Family (pdb code 6yoa). 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 Lig V 1 Structure and the Inflammatory Response to the Ole E 1 Protein Family, PDB code: 6yoa:

Nickel binding site 1 out of 1 in 6yoa

Go back to Nickel Binding Sites List in 6yoa
Nickel binding site 1 out of 1 in the Lig V 1 Structure and the Inflammatory Response to the Ole E 1 Protein Family


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Lig V 1 Structure and the Inflammatory Response to the Ole E 1 Protein Family within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ni200

b:91.5
occ:1.00
NE2 B:HIS73 1.8 0.1 1.0
OE1 B:GLU70 2.4 0.9 1.0
CE1 B:HIS73 2.5 0.8 1.0
CD2 B:HIS73 2.9 0.5 1.0
OD1 B:ASP72 3.0 0.4 1.0
OD2 B:ASP72 3.3 0.7 1.0
CD B:GLU70 3.5 0.1 1.0
CG B:ASP72 3.6 0.1 1.0
ND1 B:HIS73 3.6 0.7 1.0
CG B:HIS73 3.8 0.8 1.0
CG B:GLU70 4.2 0.9 1.0
OE2 B:GLU70 4.4 1.0 1.0
CB B:PHE53 4.7 1.0 1.0
CG B:PHE53 4.9 1.0 1.0

Reference:

T.Robledo Retana, J.Bradley-Clarke, T.Croll, R.Rose, A.J.Stagg, M.Villalba, I.Honti, R.W.Pickersgill. Lig V 1 Structure and the Inflammatory Response to the Ole E 1 Protein Family. Allergy 2020.
ISSN: ESSN 1398-9995
PubMed: 32359174
DOI: 10.1111/ALL.14351
Page generated: Wed Dec 16 01:57:13 2020

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