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Aluminium in PDB 4hna: Kinesin Motor Domain in the Adp-Mg-Alfx State in Complex with Tubulin and A Darpin

Protein crystallography data

The structure of Kinesin Motor Domain in the Adp-Mg-Alfx State in Complex with Tubulin and A Darpin, PDB code: 4hna was solved by B.Gigant, M.Knossow, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 59.14 / 3.19
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 77.050, 160.540, 174.950, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 21.1

Other elements in 4hna:

The structure of Kinesin Motor Domain in the Adp-Mg-Alfx State in Complex with Tubulin and A Darpin also contains other interesting chemical elements:

Fluorine (F) 8 atoms
Magnesium (Mg) 3 atoms

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Kinesin Motor Domain in the Adp-Mg-Alfx State in Complex with Tubulin and A Darpin (pdb code 4hna). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Kinesin Motor Domain in the Adp-Mg-Alfx State in Complex with Tubulin and A Darpin, PDB code: 4hna:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in 4hna

Go back to Aluminium Binding Sites List in 4hna
Aluminium binding site 1 out of 2 in the Kinesin Motor Domain in the Adp-Mg-Alfx State in Complex with Tubulin and A Darpin


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Kinesin Motor Domain in the Adp-Mg-Alfx State in Complex with Tubulin and A Darpin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Al503

b:93.9
occ:1.00
AL B:ALF503 0.0 93.9 1.0
F1 B:ALF503 1.8 99.1 1.0
F4 B:ALF503 1.8 86.8 1.0
F2 B:ALF503 1.8 96.0 1.0
F3 B:ALF503 1.8 98.0 1.0
O3B B:GDP501 2.1 85.3 1.0
PB B:GDP501 3.1 79.6 1.0
O2B B:GDP501 3.2 76.2 1.0
O3A B:GDP501 3.6 79.9 1.0
MG B:MG502 3.8 55.8 1.0
OG1 B:THR145 4.1 73.1 1.0
N B:ASN101 4.3 74.2 1.0
N B:ALA99 4.3 79.5 1.0
OE1 B:GLU71 4.4 0.8 1.0
N B:GLY100 4.4 79.2 1.0
N B:GLY144 4.5 67.9 1.0
O1B B:GDP501 4.5 78.6 1.0
N B:THR145 4.5 65.2 1.0
OD1 B:ASN101 4.6 74.8 1.0
CB B:ALA99 4.7 75.2 1.0
CA B:ALA99 4.8 77.0 1.0
CB B:THR145 4.9 71.0 1.0
C B:ALA99 4.9 80.8 1.0
O1A B:GDP501 4.9 74.7 1.0
PA B:GDP501 5.0 73.4 1.0
CA B:ASN101 5.0 71.6 1.0
CA B:GLY144 5.0 67.0 1.0

Aluminium binding site 2 out of 2 in 4hna

Go back to Aluminium Binding Sites List in 4hna
Aluminium binding site 2 out of 2 in the Kinesin Motor Domain in the Adp-Mg-Alfx State in Complex with Tubulin and A Darpin


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Kinesin Motor Domain in the Adp-Mg-Alfx State in Complex with Tubulin and A Darpin within 5.0Å range:
probe atom residue distance (Å) B Occ
K:Al403

b:52.8
occ:1.00
AL K:ALF403 0.0 52.8 1.0
F1 K:ALF403 1.8 50.3 1.0
F4 K:ALF403 1.8 55.5 1.0
F2 K:ALF403 1.8 54.5 1.0
F3 K:ALF403 1.8 51.4 1.0
O3B K:ADP401 1.9 55.7 1.0
PB K:ADP401 3.2 59.4 1.0
O2B K:ADP401 3.5 59.2 1.0
N K:SER202 3.5 62.5 1.0
MG K:MG402 3.6 27.4 1.0
OG K:SER201 3.7 85.0 1.0
O K:HOH502 3.9 17.7 1.0
N K:GLY234 4.0 48.9 1.0
O K:SER202 4.0 65.5 1.0
ND2 K:ASN198 4.1 61.1 1.0
N K:SER88 4.1 59.8 1.0
O3A K:ADP401 4.1 57.6 1.0
CB K:SER202 4.1 60.2 1.0
CA K:SER201 4.1 69.0 1.0
OG1 K:THR87 4.2 54.6 1.0
NZ K:LYS91 4.2 42.2 1.0
C K:SER201 4.3 70.9 1.0
O1B K:ADP401 4.3 60.3 1.0
CA K:SER202 4.3 60.3 1.0
CA K:THR87 4.4 55.5 1.0
CE K:LYS91 4.4 37.0 1.0
CB K:SER201 4.4 74.0 1.0
O K:HOH501 4.5 0.8 1.0
CA K:GLY234 4.6 49.6 1.0
C K:SER202 4.6 64.7 1.0
OG K:SER202 4.7 64.2 1.0
CB K:THR87 4.7 62.6 1.0
CA K:ALA233 4.8 46.7 1.0
C K:THR87 4.8 62.6 1.0
C K:ALA233 4.8 50.8 1.0
CA K:SER88 5.0 60.5 1.0

Reference:

B.Gigant, W.Wang, B.Dreier, Q.Jiang, L.Pecqueur, A.Pluckthun, C.Wang, M.Knossow. Structure of A Kinesin-Tubulin Complex and Implications For Kinesin Motility. Nat.Struct.Mol.Biol. V. 20 1001 2013.
ISSN: ISSN 1545-9993
PubMed: 23872990
DOI: 10.1038/NSMB.2624
Page generated: Wed Jul 10 09:45:17 2024

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