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Iron in PDB 8ghc: The Structure of H12-Lox in Dimeric Form

Enzymatic activity of The Structure of H12-Lox in Dimeric Form

All present enzymatic activity of The Structure of H12-Lox in Dimeric Form:
1.13.11.31; 1.13.11.33;

Iron Binding Sites:

The binding sites of Iron atom in the The Structure of H12-Lox in Dimeric Form (pdb code 8ghc). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the The Structure of H12-Lox in Dimeric Form, PDB code: 8ghc:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 8ghc

Go back to Iron Binding Sites List in 8ghc
Iron binding site 1 out of 2 in the The Structure of H12-Lox in Dimeric Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Structure of H12-Lox in Dimeric Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe901

b:57.0
occ:1.00
NE2 A:HIS365 2.1 35.6 1.0
NE2 A:HIS360 2.1 40.9 1.0
NE2 A:HIS540 2.1 34.0 1.0
OXT A:ILE663 2.3 56.3 1.0
CD2 A:HIS540 2.9 27.0 1.0
CE1 A:HIS360 3.0 34.0 1.0
CD2 A:HIS365 3.0 31.5 1.0
C A:ILE663 3.1 54.9 1.0
O A:ILE663 3.1 58.8 1.0
OD1 A:ASN544 3.1 35.1 1.0
CE1 A:HIS365 3.2 32.2 1.0
CD2 A:HIS360 3.2 29.7 1.0
CE1 A:HIS540 3.2 36.4 1.0
CG A:ASN544 3.6 37.3 1.0
CB A:ASN544 4.0 33.5 1.0
ND1 A:HIS360 4.1 41.9 1.0
CG A:HIS540 4.2 29.4 1.0
CG A:HIS365 4.2 34.3 1.0
ND1 A:HIS365 4.2 25.1 1.0
CG A:HIS360 4.3 34.9 1.0
ND1 A:HIS540 4.3 35.1 1.0
ND2 A:ASN544 4.4 42.2 1.0
CA A:ILE663 4.6 49.9 1.0
CG1 A:VAL661 4.6 40.0 1.0
CG2 A:ILE663 4.9 54.4 1.0
N A:ILE663 4.9 45.3 1.0

Iron binding site 2 out of 2 in 8ghc

Go back to Iron Binding Sites List in 8ghc
Iron binding site 2 out of 2 in the The Structure of H12-Lox in Dimeric Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Structure of H12-Lox in Dimeric Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe901

b:97.2
occ:1.00
OXT B:ILE663 2.1 99.0 1.0
NE2 B:HIS360 2.1 70.5 1.0
NE2 B:HIS540 2.1 68.0 1.0
NE2 B:HIS365 2.1 64.4 1.0
CD2 B:HIS540 2.5 57.1 1.0
CD2 B:HIS365 2.8 56.9 1.0
CD2 B:HIS360 2.9 67.2 1.0
C B:ILE663 3.1 95.5 1.0
CE1 B:HIS360 3.2 68.3 1.0
O B:ILE663 3.3 90.4 1.0
CE1 B:HIS365 3.3 63.7 1.0
OD1 B:ASN544 3.3 75.4 1.0
CE1 B:HIS540 3.4 69.0 1.0
CG B:HIS540 3.8 56.8 1.0
CG B:ASN544 3.9 73.1 1.0
CG B:HIS365 4.1 52.7 1.0
CG B:HIS360 4.1 58.3 1.0
CB B:ASN544 4.1 68.4 1.0
CG1 B:VAL661 4.2 73.9 1.0
ND1 B:HIS360 4.2 66.1 1.0
ND1 B:HIS540 4.2 68.9 1.0
ND1 B:HIS365 4.3 59.1 1.0
CA B:ILE663 4.5 93.3 1.0
N B:ILE663 4.7 89.5 1.0
OG1 B:THR364 4.8 73.8 1.0
ND2 B:ASN544 4.8 78.1 1.0
O B:HIS360 4.8 71.6 1.0
CG2 B:ILE663 4.9 90.5 1.0

Reference:

J.I.Mobbs, K.A.Black, M.Tran, W.A.C.Burger, H.Venugopal, T.R.Holman, M.Holinstat, D.Thal, A.Glukhova. Cryo-Em Structures of Human Arachidonate 12S-Lipoxygenase (12-Lox) Bound to Endogenous and Exogenous Inhibitors. Blood 2023.
ISSN: ESSN 1528-0020
PubMed: 37506345
DOI: 10.1182/BLOOD.2023020441
Page generated: Sat Aug 10 04:51:08 2024

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