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Iron in PDB 1dxd: Photolyzed Co Complex of Myoglobin Mb-Yqr at 20K

Protein crystallography data

The structure of Photolyzed Co Complex of Myoglobin Mb-Yqr at 20K, PDB code: 1dxd was solved by M.Brunori, B.Vallone, F.Cutruzzola, C.Travaglini-Allocatelli, J.Berendzen, K.Chu, R.M.Sweet, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18 / 1.4
Space group P 6
Cell size a, b, c (Å), α, β, γ (°) 90.493, 90.493, 45.283, 90.00, 90.00, 120.00
R / Rfree (%) 13.3 / 16.9

Iron Binding Sites:

The binding sites of Iron atom in the Photolyzed Co Complex of Myoglobin Mb-Yqr at 20K (pdb code 1dxd). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Photolyzed Co Complex of Myoglobin Mb-Yqr at 20K, PDB code: 1dxd:

Iron binding site 1 out of 1 in 1dxd

Go back to Iron Binding Sites List in 1dxd
Iron binding site 1 out of 1 in the Photolyzed Co Complex of Myoglobin Mb-Yqr at 20K


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Photolyzed Co Complex of Myoglobin Mb-Yqr at 20K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe154

b:8.0
occ:1.00
FE A:HEM154 0.0 8.0 1.0
NB A:HEM154 2.0 7.3 1.0
NA A:HEM154 2.0 7.9 1.0
NC A:HEM154 2.0 7.2 1.0
ND A:HEM154 2.0 7.6 1.0
NE2 A:HIS93 2.1 7.7 1.0
C1C A:HEM154 3.1 7.6 1.0
C4B A:HEM154 3.1 8.1 1.0
C1A A:HEM154 3.1 8.3 1.0
C4A A:HEM154 3.1 7.5 1.0
C1B A:HEM154 3.1 6.8 1.0
CE1 A:HIS93 3.1 8.1 1.0
C1D A:HEM154 3.1 8.5 1.0
C4D A:HEM154 3.1 6.9 1.0
C4C A:HEM154 3.1 6.9 1.0
CD2 A:HIS93 3.2 8.3 1.0
CHC A:HEM154 3.4 8.4 1.0
CHA A:HEM154 3.5 8.9 1.0
CHB A:HEM154 3.5 8.7 1.0
CHD A:HEM154 3.5 8.8 1.0
ND1 A:HIS93 4.3 8.6 1.0
C3A A:HEM154 4.3 6.2 1.0
C2B A:HEM154 4.3 7.3 1.0
C2A A:HEM154 4.3 7.3 1.0
CG A:HIS93 4.3 7.4 1.0
C3B A:HEM154 4.3 7.1 1.0
C2D A:HEM154 4.3 8.5 1.0
C2C A:HEM154 4.3 7.7 1.0
C3D A:HEM154 4.3 9.2 1.0
C3C A:HEM154 4.3 8.2 1.0
CG2 A:VAL68 4.4 10.3 1.0

Reference:

M.Brunori, B.Vallone, F.Cutruzzola, C.Travaglini-Allocatelli, J.Berendzen, K.Chu, R.M.Sweet, I.Schlichting. The Role of Cavities in Protein Dynamics: Crystal Structure of A Photolytic Intermediate of A Mutant Myoglobin. Proc.Natl.Acad.Sci.Usa V. 97 2058 2000.
ISSN: ISSN 0027-8424
PubMed: 10681426
DOI: 10.1073/PNAS.040459697
Page generated: Sun Dec 13 14:11:34 2020

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