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Iron in PDB 1v75: Crystal Structure of Hemoglobin D From the Aldabra Giant Tortoise (Geochelone Gigantea) at 2.0 A Resolution

Protein crystallography data

The structure of Crystal Structure of Hemoglobin D From the Aldabra Giant Tortoise (Geochelone Gigantea) at 2.0 A Resolution, PDB code: 1v75 was solved by T.Kuwada, T.Hasegawa, I.Satoh, K.Ishikawa, F.Shishikura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.96 / 2.02
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 112.142, 62.374, 53.980, 90.00, 110.26, 90.00
R / Rfree (%) n/a / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Hemoglobin D From the Aldabra Giant Tortoise (Geochelone Gigantea) at 2.0 A Resolution (pdb code 1v75). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Hemoglobin D From the Aldabra Giant Tortoise (Geochelone Gigantea) at 2.0 A Resolution, PDB code: 1v75:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1v75

Go back to Iron Binding Sites List in 1v75
Iron binding site 1 out of 2 in the Crystal Structure of Hemoglobin D From the Aldabra Giant Tortoise (Geochelone Gigantea) at 2.0 A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Hemoglobin D From the Aldabra Giant Tortoise (Geochelone Gigantea) at 2.0 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:24.6
occ:1.00
FE A:HEM201 0.0 24.6 1.0
NB A:HEM201 2.0 25.2 1.0
NC A:HEM201 2.1 23.2 1.0
NA A:HEM201 2.1 29.4 1.0
ND A:HEM201 2.1 24.9 1.0
O A:HOH451 2.2 20.1 1.0
NE2 A:HIS87 2.2 22.5 1.0
C4B A:HEM201 3.0 25.1 1.0
C1C A:HEM201 3.0 22.8 1.0
C1A A:HEM201 3.1 29.3 1.0
C1B A:HEM201 3.1 26.9 1.0
C4D A:HEM201 3.1 24.4 1.0
C4A A:HEM201 3.1 30.3 1.0
C4C A:HEM201 3.1 21.9 1.0
C1D A:HEM201 3.1 23.5 1.0
CE1 A:HIS87 3.2 25.1 1.0
CD2 A:HIS87 3.2 22.4 1.0
CHC A:HEM201 3.4 21.2 1.0
CHA A:HEM201 3.4 26.2 1.0
CHB A:HEM201 3.5 27.3 1.0
CHD A:HEM201 3.5 22.2 1.0
C3B A:HEM201 4.3 26.0 1.0
NE2 A:HIS58 4.3 21.0 1.0
C2B A:HEM201 4.3 27.8 1.0
C2C A:HEM201 4.3 20.8 1.0
C2A A:HEM201 4.3 29.9 1.0
C3C A:HEM201 4.3 22.6 1.0
C3D A:HEM201 4.3 22.8 1.0
ND1 A:HIS87 4.3 23.9 1.0
C3A A:HEM201 4.3 30.5 1.0
C2D A:HEM201 4.3 22.0 1.0
CG A:HIS87 4.4 22.8 1.0
CE1 A:HIS58 4.4 24.1 1.0

Iron binding site 2 out of 2 in 1v75

Go back to Iron Binding Sites List in 1v75
Iron binding site 2 out of 2 in the Crystal Structure of Hemoglobin D From the Aldabra Giant Tortoise (Geochelone Gigantea) at 2.0 A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Hemoglobin D From the Aldabra Giant Tortoise (Geochelone Gigantea) at 2.0 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe201

b:31.3
occ:1.00
FE B:HEM201 0.0 31.3 1.0
O B:HOH363 2.0 25.3 1.0
NB B:HEM201 2.0 30.8 1.0
NC B:HEM201 2.1 32.1 1.0
NA B:HEM201 2.1 34.0 1.0
ND B:HEM201 2.1 35.7 1.0
NE2 B:HIS92 2.2 32.1 1.0
C4B B:HEM201 3.0 31.1 1.0
C1C B:HEM201 3.0 31.1 1.0
C1B B:HEM201 3.0 33.8 1.0
C1A B:HEM201 3.1 35.5 1.0
C4D B:HEM201 3.1 36.8 1.0
C4A B:HEM201 3.1 34.3 1.0
CD2 B:HIS92 3.1 33.3 1.0
C4C B:HEM201 3.1 33.6 1.0
C1D B:HEM201 3.1 35.9 1.0
CE1 B:HIS92 3.3 32.1 1.0
CHC B:HEM201 3.4 30.5 1.0
CHA B:HEM201 3.4 35.3 1.0
CHB B:HEM201 3.5 33.0 1.0
CHD B:HEM201 3.5 34.7 1.0
C3B B:HEM201 4.3 32.3 1.0
NE2 B:HIS63 4.3 29.3 1.0
C2B B:HEM201 4.3 33.5 1.0
C2C B:HEM201 4.3 31.2 1.0
C2A B:HEM201 4.3 35.8 1.0
CG B:HIS92 4.3 33.9 1.0
C3C B:HEM201 4.3 33.9 1.0
C3A B:HEM201 4.3 35.3 1.0
C3D B:HEM201 4.3 37.5 1.0
C2D B:HEM201 4.3 36.5 1.0
ND1 B:HIS92 4.4 31.9 1.0
CG2 B:VAL67 4.5 20.3 1.0
CE1 B:HIS63 4.5 28.4 1.0

Reference:

T.Kuwada, T.Hasegawa, I.Satoh, K.Ishikawa, F.Shishikura. Crystallization and Preliminary X-Ray Diffraction Study of Hemoglobin D From the Aldabra Giant Tortoise, Geochelone Gigantea. Protein Pept.Lett. V. 10 422 2003.
ISSN: ISSN 0929-8665
PubMed: 14529497
DOI: 10.2174/0929866033478799
Page generated: Sat Aug 3 16:09:54 2024

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