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Aluminium in PDB 4iyn: Structure of Mitochondrial HSP90 (TRAP1) with Adp-ALF4-

Protein crystallography data

The structure of Structure of Mitochondrial HSP90 (TRAP1) with Adp-ALF4-, PDB code: 4iyn was solved by J.R.Partridge, L.A.Lavery, D.A.Agard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.81 / 2.31
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 178.896, 96.597, 125.901, 90.00, 134.26, 90.00
R / Rfree (%) 19.1 / 23.1

Other elements in 4iyn:

The structure of Structure of Mitochondrial HSP90 (TRAP1) with Adp-ALF4- also contains other interesting chemical elements:

Fluorine (F) 8 atoms
Cobalt (Co) 4 atoms
Magnesium (Mg) 2 atoms

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Structure of Mitochondrial HSP90 (TRAP1) with Adp-ALF4- (pdb code 4iyn). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Structure of Mitochondrial HSP90 (TRAP1) with Adp-ALF4-, PDB code: 4iyn:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in 4iyn

Go back to Aluminium Binding Sites List in 4iyn
Aluminium binding site 1 out of 2 in the Structure of Mitochondrial HSP90 (TRAP1) with Adp-ALF4-


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Structure of Mitochondrial HSP90 (TRAP1) with Adp-ALF4- within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al803

b:33.0
occ:1.00
AL A:ALF803 0.0 33.0 1.0
F1 A:ALF803 1.8 33.9 1.0
O1B A:ADP802 1.8 33.2 1.0
F3 A:ALF803 1.8 29.4 1.0
F2 A:ALF803 1.8 32.5 1.0
F4 A:ALF803 1.8 31.6 1.0
O A:HOH994 2.3 27.6 1.0
MG A:MG804 3.0 37.1 1.0
PB A:ADP802 3.0 39.6 1.0
O2B A:ADP802 3.5 36.4 1.0
O3A A:ADP802 3.6 30.6 1.0
N A:GLY219 3.7 37.9 1.0
OE1 A:GLU130 3.9 39.2 1.0
N A:GLY217 4.0 38.3 1.0
O A:HOH1025 4.0 31.3 1.0
O1A A:ADP802 4.0 27.0 1.0
NH2 A:ARG417 4.0 42.1 1.0
CA A:GLY219 4.1 36.4 1.0
N A:PHE216 4.1 36.8 1.0
NE A:ARG417 4.1 41.7 1.0
O A:HOH964 4.2 44.3 1.0
N A:GLN215 4.2 47.3 1.0
O A:HOH995 4.2 33.4 1.0
N A:VAL218 4.3 37.9 1.0
O3B A:ADP802 4.3 39.1 1.0
O A:HOH957 4.3 32.8 1.0
PA A:ADP802 4.4 36.8 1.0
CA A:GLY214 4.4 38.4 1.0
CZ A:ARG417 4.5 41.0 1.0
CB A:PHE216 4.5 36.8 1.0
CA A:PHE216 4.6 37.6 1.0
C A:PHE216 4.7 39.3 1.0
CA A:GLY217 4.7 40.9 1.0
C A:VAL218 4.8 37.1 1.0
C A:GLY214 4.8 38.1 1.0
C A:GLN215 4.9 48.8 1.0
CD2 A:PHE216 4.9 34.6 1.0
O2A A:ADP802 5.0 34.6 1.0
C A:GLY217 5.0 42.2 1.0

Aluminium binding site 2 out of 2 in 4iyn

Go back to Aluminium Binding Sites List in 4iyn
Aluminium binding site 2 out of 2 in the Structure of Mitochondrial HSP90 (TRAP1) with Adp-ALF4-


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Structure of Mitochondrial HSP90 (TRAP1) with Adp-ALF4- within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Al804

b:50.1
occ:0.86
AL B:ALF804 0.0 50.1 0.9
F3 B:ALF804 1.8 50.1 0.9
F2 B:ALF804 1.8 51.6 0.9
F4 B:ALF804 1.8 46.9 0.9
O1B B:ADP803 1.8 59.1 1.0
F1 B:ALF804 1.8 50.6 0.9
O B:HOH1036 2.2 44.9 1.0
PB B:ADP803 3.0 47.0 1.0
MG B:MG805 3.2 52.5 1.0
O2B B:ADP803 3.3 41.0 1.0
O3A B:ADP803 3.5 56.7 1.0
O B:HOH1049 3.8 58.2 1.0
NH2 B:ARG417 3.8 56.6 1.0
N B:GLY219 3.8 38.0 1.0
OE1 B:GLU130 3.9 48.6 1.0
NE B:ARG417 4.0 55.3 1.0
N B:GLY217 4.1 51.5 1.0
N B:PHE216 4.1 48.0 1.0
O1A B:ADP803 4.1 44.6 1.0
CA B:GLY219 4.1 38.0 1.0
O B:HOH931 4.1 44.7 1.0
CA B:GLY214 4.1 48.2 1.0
N B:GLN215 4.2 58.1 1.0
O3B B:ADP803 4.3 48.5 1.0
O B:HOH917 4.3 48.7 1.0
O B:HOH983 4.3 50.3 1.0
CZ B:ARG417 4.4 55.1 1.0
CB B:PHE216 4.4 48.0 1.0
PA B:ADP803 4.4 44.8 1.0
N B:VAL218 4.4 45.2 1.0
CA B:PHE216 4.6 48.5 1.0
C B:GLY214 4.6 48.4 1.0
C B:PHE216 4.8 49.4 1.0
CA B:GLY217 4.9 52.9 1.0
C B:GLN215 5.0 59.1 1.0

Reference:

L.A.Lavery, J.R.Partridge, T.A.Ramelot, D.Elnatan, M.A.Kennedy, D.A.Agard. Structural Asymmetry in the Closed State of Mitochondrial HSP90 (TRAP1) Supports A Two-Step Atp Hydrolysis Mechanism. Mol.Cell V. 53 330 2014.
ISSN: ISSN 1097-2765
PubMed: 24462206
DOI: 10.1016/J.MOLCEL.2013.12.023
Page generated: Sun Jul 6 21:53:57 2025

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