Iron in PDB 6h6u: Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition)

Enzymatic activity of Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition)

All present enzymatic activity of Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition):
1.16.3.1;

Protein crystallography data

The structure of Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition), PDB code: 6h6u was solved by M.Kuenzle, M.Lach, T.Beck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.17 / 2.00
Space group I 4
Cell size a, b, c (Å), α, β, γ (°) 124.682, 124.682, 188.674, 90.00, 90.00, 90.00
R / Rfree (%) 23.8 / 30.8

Other elements in 6h6u:

The structure of Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition) also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Iron Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 15;

Binding sites:

The binding sites of Iron atom in the Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition) (pdb code 6h6u). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 15 binding sites of Iron where determined in the Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition), PDB code: 6h6u:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 15 in 6h6u

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Iron binding site 1 out of 15 in the Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:65.7
occ:1.00
OE1 A:GLU62 1.9 50.3 1.0
OE1 A:GLU27 2.3 56.2 1.0
O A:HOH312 2.4 67.8 1.0
O A:HOH309 2.5 53.2 1.0
CD2 A:HIS65 2.6 59.6 1.0
CD A:GLU62 2.9 49.3 1.0
CD A:GLU27 3.2 54.1 1.0
OE2 A:GLU62 3.2 55.6 1.0
CG A:HIS65 3.4 60.4 1.0
OE2 A:GLU27 3.4 45.9 1.0
NE2 A:HIS65 3.6 67.1 1.0
OE1 A:GLN141 3.7 54.8 1.0
CB A:HIS65 3.8 53.3 1.0
CG A:GLU62 4.3 41.1 1.0
OE1 A:GLU107 4.4 62.3 1.0
CG1 A:VAL110 4.5 54.8 1.0
ND1 A:HIS65 4.5 66.7 1.0
CE1 A:HIS65 4.6 59.0 1.0
CG A:GLU27 4.6 47.4 1.0
CA A:GLU62 4.7 44.2 1.0
CB A:GLU62 4.7 42.8 1.0
OE2 A:GLU107 4.8 64.9 1.0
CD A:GLN141 4.8 50.2 1.0

Iron binding site 2 out of 15 in 6h6u

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Iron binding site 2 out of 15 in the Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe202

b:84.3
occ:1.00
OE1 A:GLN58 2.5 64.7 1.0
O A:HOH315 2.5 55.0 1.0
OE1 A:GLU61 2.7 63.9 1.0
OE2 A:GLU62 3.0 55.6 1.0
CD A:GLU61 3.5 64.6 1.0
OE2 A:GLU140 3.6 67.7 1.0
CD A:GLN58 3.6 54.4 1.0
OE2 A:GLU107 3.7 64.9 1.0
O A:HOH309 3.8 53.2 1.0
CG A:GLU61 4.1 53.6 1.0
OE2 A:GLU61 4.2 72.4 1.0
CD A:GLU62 4.3 49.3 1.0
CB A:GLN58 4.4 42.2 1.0
CG A:GLN58 4.4 45.8 1.0
CB A:ALA144 4.5 40.0 1.0
CA A:GLN58 4.6 38.7 1.0
CD A:GLU107 4.6 62.5 1.0
NE2 A:GLN58 4.6 63.2 1.0
CB A:GLU61 4.7 46.7 1.0
CE2 A:TYR34 4.7 43.4 1.0
NE2 A:HIS65 4.7 67.1 1.0
OH A:TYR34 4.8 58.9 1.0
O A:GLN58 4.8 39.9 1.0
CD A:GLU140 4.9 68.4 1.0
CZ A:TYR34 5.0 53.4 1.0
CG A:GLU62 5.0 41.1 1.0

Iron binding site 3 out of 15 in 6h6u

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Iron binding site 3 out of 15 in the Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe203

b:89.1
occ:1.00
OE2 A:GLU61 2.6 72.4 1.0
OE1 A:GLU61 3.1 63.9 1.0
CD A:GLU61 3.2 64.6 1.0
NE2 A:HIS57 4.2 51.7 1.0
OE1 A:GLU140 4.2 64.5 1.0
OE2 A:GLU140 4.3 67.7 1.0
CG A:GLU61 4.6 53.6 1.0
CD A:GLU140 4.7 68.4 1.0
CD2 A:HIS57 4.9 45.5 1.0

Iron binding site 4 out of 15 in 6h6u

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Iron binding site 4 out of 15 in the Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe201

b:71.8
occ:1.00
OE1 B:GLU62 1.9 59.1 1.0
OE1 B:GLU27 2.5 56.8 1.0
ND1 B:HIS65 2.6 57.3 1.0
CD B:GLU62 2.7 61.8 1.0
OE2 B:GLU62 2.8 70.6 1.0
CD B:GLU27 3.3 50.2 1.0
OE1 B:GLN141 3.3 64.2 1.0
CE1 B:HIS65 3.4 60.5 1.0
OE2 B:GLU27 3.4 53.5 1.0
O B:HOH309 3.5 69.5 1.0
CG B:HIS65 3.7 58.1 1.0
CB B:HIS65 4.0 54.0 1.0
CG B:GLU62 4.1 54.2 1.0
OE1 B:GLU107 4.1 72.0 1.0
CD B:GLN141 4.2 63.1 1.0
CG1 B:VAL110 4.4 70.8 1.0
NE2 B:HIS65 4.6 61.3 1.0
NE2 B:GLN141 4.7 65.1 1.0
CG B:GLU27 4.7 47.9 1.0
CA B:GLU62 4.7 52.9 1.0
CD2 B:HIS65 4.7 61.6 1.0
CB B:GLU62 4.7 53.3 1.0
OE2 B:GLU107 4.8 69.0 1.0
CD B:GLU107 4.9 68.2 1.0

Iron binding site 5 out of 15 in 6h6u

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Iron binding site 5 out of 15 in the Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe202

b:93.3
occ:1.00
OE1 B:GLN58 2.4 71.7 1.0
OE2 B:GLU61 2.5 75.2 1.0
O B:HOH309 3.1 69.5 1.0
CD B:GLU61 3.2 75.8 1.0
CD B:GLN58 3.3 54.8 1.0
OE2 B:GLU62 3.5 70.6 1.0
NE2 B:GLN58 3.7 55.4 1.0
OE1 B:GLU61 3.7 77.5 1.0
OE2 B:GLU107 3.7 69.0 1.0
CG B:GLU61 4.1 68.4 1.0
OE2 B:GLU140 4.4 64.8 1.0
CB B:GLU61 4.4 58.5 1.0
CG B:GLN58 4.4 49.4 1.0
CB B:GLN58 4.5 44.4 1.0
CA B:GLN58 4.5 43.1 1.0
O B:GLN58 4.6 48.9 1.0
CB B:ALA144 4.6 44.4 1.0
CD B:GLU62 4.6 61.8 1.0
CD B:GLU107 4.6 68.2 1.0
OH B:TYR34 4.9 57.4 1.0
CE2 B:TYR34 4.9 48.3 1.0
CE1 B:HIS65 5.0 60.5 1.0

Iron binding site 6 out of 15 in 6h6u

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Iron binding site 6 out of 15 in the Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe203

b:95.7
occ:1.00
OE1 B:GLU61 2.8 77.5 1.0
CD B:GLU61 3.3 75.8 1.0
OE2 B:GLU61 3.4 75.2 1.0
OE2 B:GLU140 4.2 64.8 1.0
NE2 B:HIS57 4.3 64.4 1.0
CG B:GLU61 4.5 68.4 1.0
OE1 B:GLU140 4.8 63.0 1.0
CD B:GLU140 4.9 62.8 1.0

Iron binding site 7 out of 15 in 6h6u

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Iron binding site 7 out of 15 in the Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe201

b:80.5
occ:1.00
OE1 C:GLU62 2.0 52.5 1.0
OE1 C:GLU27 2.3 55.2 1.0
CD C:GLU62 2.8 54.2 1.0
ND1 C:HIS65 2.9 68.6 1.0
OE2 C:GLU62 2.9 58.6 1.0
OE1 C:GLN141 2.9 77.2 1.0
CD C:GLU27 3.2 52.9 1.0
OE2 C:GLU27 3.3 57.0 1.0
CE1 C:HIS65 3.4 69.9 1.0
CG C:HIS65 3.6 57.2 1.0
OE1 C:GLU107 3.9 96.1 1.0
CD C:GLN141 4.0 71.0 1.0
CB C:HIS65 4.0 52.8 1.0
CG1 C:VAL110 4.1 73.6 1.0
CG C:GLU62 4.2 44.7 1.0
NE2 C:HIS65 4.3 74.2 1.0
CD2 C:HIS65 4.4 67.2 1.0
OE2 C:GLU107 4.5 94.4 1.0
NE2 C:GLN141 4.5 66.6 1.0
CG C:GLU27 4.6 44.6 1.0
CD C:GLU107 4.7 84.5 1.0
CB C:GLU62 4.8 47.4 1.0
CA C:GLU62 4.9 46.9 1.0

Iron binding site 8 out of 15 in 6h6u

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Iron binding site 8 out of 15 in the Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe202

b:98.2
occ:1.00
OE1 C:GLN58 2.5 63.1 1.0
OE2 C:GLU62 3.3 58.6 1.0
OE2 C:GLU61 3.3 66.8 1.0
OE1 C:GLU140 3.3 83.7 1.0
CD C:GLU61 3.5 66.4 1.0
CD C:GLN58 3.7 59.3 1.0
CG C:GLU61 4.0 63.6 1.0
OE1 C:GLU107 4.1 96.1 1.0
OE1 C:GLU61 4.2 75.7 1.0
OE2 C:GLU107 4.2 94.4 1.0
CB C:ALA144 4.2 51.0 1.0
CD C:GLU107 4.3 84.5 1.0
CD C:GLU62 4.4 54.2 1.0
CB C:GLU61 4.5 55.2 1.0
CD C:GLU140 4.5 75.8 1.0
CE1 C:HIS65 4.6 69.9 1.0
CG C:GLN58 4.6 49.8 1.0
NE2 C:GLN58 4.6 56.3 1.0
CB C:GLN58 4.7 47.8 1.0
OH C:TYR34 4.7 59.7 1.0
CA C:GLN58 4.8 52.7 1.0
O C:GLN58 4.9 45.5 1.0
CG C:GLU62 5.0 44.7 1.0
CE2 C:TYR34 5.0 58.9 1.0

Iron binding site 9 out of 15 in 6h6u

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Iron binding site 9 out of 15 in the Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe201

b:70.6
occ:1.00
OE1 D:GLU62 2.0 40.1 1.0
OE1 D:GLU27 2.4 59.5 1.0
ND1 D:HIS65 2.6 59.0 1.0
CD D:GLU62 2.9 45.5 1.0
OE2 D:GLU62 3.1 53.6 1.0
OE1 D:GLN141 3.2 64.7 1.0
CE1 D:HIS65 3.2 60.7 1.0
CD D:GLU27 3.2 48.1 1.0
OE2 D:GLU27 3.3 44.7 1.0
CG D:HIS65 3.5 52.7 1.0
CB D:HIS65 4.0 41.5 1.0
CG1 D:VAL110 4.1 57.7 1.0
NE2 D:HIS65 4.3 60.6 1.0
CD D:GLN141 4.3 55.4 1.0
OE1 D:GLU107 4.3 88.6 1.0
CG D:GLU62 4.4 44.9 1.0
CD2 D:HIS65 4.5 60.8 1.0
CG D:GLU27 4.7 50.1 1.0
CD2 D:TYR137 4.8 46.1 1.0
CE2 D:TYR137 4.9 43.0 1.0
FE D:FE202 4.9 0.1 1.0
CA D:GLU62 4.9 47.1 1.0
OE2 D:GLU107 5.0 70.1 1.0
CB D:GLU62 5.0 47.6 1.0

Iron binding site 10 out of 15 in 6h6u

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Iron binding site 10 out of 15 in the Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Unitary Crystal Structure of the Positively Supercharged Variant Ftn(Pos) From Human Heavy Chain Ferritin (Peg 400 Condition) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe202

b:0.1
occ:1.00
OE2 D:GLU62 2.6 53.6 1.0
OE2 D:GLU61 2.7 67.8 1.0
OE1 D:GLN58 2.7 70.8 1.0
OE2 D:GLU140 3.3 70.5 1.0
OE2 D:GLU107 3.4 70.1 1.0
CD D:GLU61 3.5 63.0 1.0
CD D:GLN58 3.6 61.0 1.0
NE2 D:GLN58 3.7 65.7 1.0
CD D:GLU62 3.9 45.5 1.0
CD D:GLU107 3.9 73.2 1.0
CB D:ALA144 4.1 37.6 1.0
CG D:GLU61 4.1 60.4 1.0
OE1 D:GLU107 4.2 88.6 1.0
CE1 D:HIS65 4.3 60.7 1.0
OE1 D:GLU61 4.3 68.3 1.0
CD D:GLU140 4.6 69.4 1.0
OE1 D:GLU62 4.7 40.1 1.0
CG D:GLU62 4.7 44.9 1.0
CG D:GLU107 4.8 63.7 1.0
OE1 D:GLN141 4.8 64.7 1.0
OH D:TYR34 4.9 54.7 1.0
ND1 D:HIS65 4.9 59.0 1.0
FE D:FE201 4.9 70.6 1.0
CG D:GLN58 5.0 50.1 1.0

Reference:

M.Kuenzle, M.Lach, T.Beck. Self-Assembly of Protein Crystals Into Different Crystal Structures Using Charged Patches on Oppositely Charged Ferritin Protein Containers To Be Published.
Page generated: Sun Dec 13 16:28:22 2020

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