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Nickel in PDB 1zx8: Crystal Structure of An Atypical Cyclophilin (Peptidylprolyl Cis-Trans Isomerase) (TM1367) From Thermotoga Maritima at 1.90 A Resolution

Protein crystallography data

The structure of Crystal Structure of An Atypical Cyclophilin (Peptidylprolyl Cis-Trans Isomerase) (TM1367) From Thermotoga Maritima at 1.90 A Resolution, PDB code: 1zx8 was solved by Joint Center For Structural Genomics (Jcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.07 / 1.90
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 77.083, 132.875, 41.319, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 21

Nickel Binding Sites:

The binding sites of Nickel atom in the Crystal Structure of An Atypical Cyclophilin (Peptidylprolyl Cis-Trans Isomerase) (TM1367) From Thermotoga Maritima at 1.90 A Resolution (pdb code 1zx8). 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 Crystal Structure of An Atypical Cyclophilin (Peptidylprolyl Cis-Trans Isomerase) (TM1367) From Thermotoga Maritima at 1.90 A Resolution, PDB code: 1zx8:

Nickel binding site 1 out of 1 in 1zx8

Go back to Nickel Binding Sites List in 1zx8
Nickel binding site 1 out of 1 in the Crystal Structure of An Atypical Cyclophilin (Peptidylprolyl Cis-Trans Isomerase) (TM1367) From Thermotoga Maritima at 1.90 A Resolution


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Crystal Structure of An Atypical Cyclophilin (Peptidylprolyl Cis-Trans Isomerase) (TM1367) From Thermotoga Maritima at 1.90 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ni125

b:39.0
occ:0.50
NE2 C:HIS-1 2.4 34.6 1.0
O C:HOH134 2.4 38.7 0.5
O C:HOH160 2.4 29.4 0.5
CE1 C:HIS-1 3.3 49.9 1.0
CD2 C:HIS-1 3.3 40.1 1.0
ND1 C:HIS-1 4.4 52.5 1.0
CG C:HIS-1 4.5 39.4 1.0

Reference:

K.K.Jin, S.S.Krishna, R.Schwarzenbacher, D.Mcmullan, P.Abdubek, S.Agarwalla, E.Ambing, H.Axelrod, J.M.Canaves, H.J.Chiu, A.M.Deacon, M.Didonato, M.A.Elsliger, J.Feuerhelm, A.Godzik, C.Grittini, S.K.Grzechnik, J.Hale, E.Hampton, J.Haugen, M.Hornsby, L.Jaroszewski, H.E.Klock, M.W.Knuth, E.Koesema, A.Kreusch, P.Kuhn, S.A.Lesley, M.D.Miller, K.Moy, E.Nigoghossian, L.Okach, S.Oommachen, J.Paulsen, K.Quijano, R.Reyes, C.Rife, R.C.Stevens, G.Spraggon, H.Van Den Bedem, J.Velasquez, A.White, G.Wolf, G.W.Han, Q.Xu, K.O.Hodgson, J.Wooley, I.A.Wilson. Crystal Structure of TM1367 From Thermotoga Maritima at 1.90 A Resolution Reveals An Atypical Member of the Cyclophilin (Peptidylprolyl Isomerase) Fold. Proteins V. 63 1112 2006.
ISSN: ISSN 0887-3585
PubMed: 16544291
DOI: 10.1002/PROT.20894
Page generated: Thu Oct 29 06:16:29 2020
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