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Iron in PDB 1fp4: Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase

Enzymatic activity of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase

All present enzymatic activity of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase:
1.18.6.1;

Protein crystallography data

The structure of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase, PDB code: 1fp4 was solved by M.Sorlie, J.Christiansen, B.J.Lemon, J.W.Peters, D.R.Dean, B.J.Hales, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 107.200, 130.200, 80.400, 90.00, 111.20, 90.00
R / Rfree (%) 18.4 / 24

Other elements in 1fp4:

The structure of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase also contains other interesting chemical elements:

Molybdenum (Mo) 2 atoms
Calcium (Ca) 2 atoms

Iron Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30;

Binding sites:

The binding sites of Iron atom in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase (pdb code 1fp4). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 30 binding sites of Iron where determined in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase, PDB code: 1fp4:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 30 in 1fp4

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Iron binding site 1 out of 30 in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase


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 the Alpha-H195Q Mutant of Nitrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe496

b:32.6
occ:1.00
FE1 A:CFM496 0.0 32.6 1.0
S2A A:CFM496 2.3 28.2 1.0
S4A A:CFM496 2.3 30.6 1.0
S1A A:CFM496 2.3 31.2 1.0
SG A:CYS275 2.3 31.2 1.0
FE2 A:CFM496 2.7 28.2 1.0
FE3 A:CFM496 2.7 29.4 1.0
FE4 A:CFM496 2.8 30.0 1.0
CB A:CYS275 3.4 34.3 1.0
OG A:SER278 3.8 37.3 1.0
CB A:LEU358 4.1 28.0 1.0
CE1 A:TYR229 4.4 36.0 1.0
CB A:SER278 4.4 36.2 1.0
CA A:CYS275 4.6 35.8 1.0
CD2 A:LEU358 4.7 20.5 1.0
CD1 A:TYR229 4.7 33.2 1.0
N A:LEU358 4.9 28.6 1.0
S2B A:CFM496 4.9 30.2 1.0
FE7 A:CFM496 4.9 28.5 1.0
S5 A:CFM496 4.9 27.4 1.0
FE6 A:CFM496 4.9 28.0 1.0
FE5 A:CFM496 5.0 26.6 1.0

Iron binding site 2 out of 30 in 1fp4

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Iron binding site 2 out of 30 in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase


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 the Alpha-H195Q Mutant of Nitrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe496

b:28.2
occ:1.00
FE2 A:CFM496 0.0 28.2 1.0
S2B A:CFM496 2.3 30.2 1.0
S1A A:CFM496 2.3 31.2 1.0
S2A A:CFM496 2.3 28.2 1.0
FE6 A:CFM496 2.5 28.0 1.0
FE1 A:CFM496 2.7 32.6 1.0
FE3 A:CFM496 2.7 29.4 1.0
FE4 A:CFM496 2.8 30.0 1.0
FE7 A:CFM496 3.6 28.5 1.0
FE5 A:CFM496 3.7 26.6 1.0
CZ A:PHE381 3.8 26.9 1.0
NE2 A:GLN195 3.8 34.5 1.0
S4A A:CFM496 3.9 30.6 1.0
S1B A:CFM496 4.2 27.4 1.0
S3B A:CFM496 4.3 22.9 1.0
CE1 A:PHE381 4.3 30.9 1.0
S5 A:CFM496 4.6 27.4 1.0
NH2 A:ARG96 4.7 28.8 1.0
SG A:CYS275 4.7 31.2 1.0
S3A A:CFM496 4.7 29.2 1.0
CG2 A:VAL70 4.8 27.9 1.0
CG1 A:VAL70 4.8 26.4 1.0
CB A:VAL70 4.9 31.9 1.0
CE2 A:PHE381 4.9 24.7 1.0
CB A:SER278 5.0 36.2 1.0

Iron binding site 3 out of 30 in 1fp4

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Iron binding site 3 out of 30 in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe496

b:29.4
occ:1.00
FE3 A:CFM496 0.0 29.4 1.0
S5 A:CFM496 2.3 27.4 1.0
S2A A:CFM496 2.3 28.2 1.0
S4A A:CFM496 2.3 30.6 1.0
FE7 A:CFM496 2.5 28.5 1.0
FE1 A:CFM496 2.7 32.6 1.0
FE2 A:CFM496 2.7 28.2 1.0
FE4 A:CFM496 2.8 30.0 1.0
FE6 A:CFM496 3.7 28.0 1.0
FE5 A:CFM496 3.7 26.6 1.0
NH2 A:ARG96 3.7 28.8 1.0
O A:HOH551 3.8 56.4 1.0
S1A A:CFM496 3.9 31.2 1.0
CD1 A:TYR229 4.0 33.2 1.0
S4B A:CFM496 4.2 25.4 1.0
S3B A:CFM496 4.3 22.9 1.0
CE1 A:TYR229 4.4 36.0 1.0
S2B A:CFM496 4.7 30.2 1.0
S3A A:CFM496 4.8 29.2 1.0
NH2 A:ARG359 4.8 32.3 1.0
CG A:TYR229 4.9 32.5 1.0
SG A:CYS275 4.9 31.2 1.0

Iron binding site 4 out of 30 in 1fp4

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Iron binding site 4 out of 30 in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe496

b:30.0
occ:1.00
FE4 A:CFM496 0.0 30.0 1.0
S1A A:CFM496 2.3 31.2 1.0
S3A A:CFM496 2.3 29.2 1.0
S4A A:CFM496 2.3 30.6 1.0
FE5 A:CFM496 2.5 26.6 1.0
FE1 A:CFM496 2.8 32.6 1.0
FE3 A:CFM496 2.8 29.4 1.0
FE2 A:CFM496 2.8 28.2 1.0
FE7 A:CFM496 3.7 28.5 1.0
FE6 A:CFM496 3.7 28.0 1.0
N A:LEU358 3.9 28.6 1.0
N A:GLY357 3.9 26.6 1.0
S2A A:CFM496 4.0 28.2 1.0
CB A:LEU358 4.1 28.0 1.0
S4B A:CFM496 4.2 25.4 1.0
S1B A:CFM496 4.2 27.4 1.0
N A:ARG359 4.5 32.6 1.0
C A:GLY357 4.5 29.8 1.0
CA A:LEU358 4.5 29.7 1.0
CD A:ARG359 4.6 27.6 1.0
CA A:GLY357 4.6 27.4 1.0
S5 A:CFM496 4.6 27.4 1.0
CZ A:PHE381 4.7 26.9 1.0
S2B A:CFM496 4.7 30.2 1.0
SG A:CYS275 4.8 31.2 1.0
C A:GLY356 4.9 27.2 1.0
NE A:ARG359 4.9 25.2 1.0

Iron binding site 5 out of 30 in 1fp4

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Iron binding site 5 out of 30 in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe496

b:26.6
occ:1.00
FE5 A:CFM496 0.0 26.6 1.0
S4B A:CFM496 2.3 25.4 1.0
S3A A:CFM496 2.3 29.2 1.0
S1B A:CFM496 2.3 27.4 1.0
FE4 A:CFM496 2.5 30.0 1.0
FE7 A:CFM496 2.7 28.5 1.0
FE6 A:CFM496 2.7 28.0 1.0
MO1 A:CFM496 2.8 27.8 1.0
FE2 A:CFM496 3.7 28.2 1.0
FE3 A:CFM496 3.7 29.4 1.0
CG2 A:ILE355 3.8 29.3 1.0
S3B A:CFM496 3.9 22.9 1.0
ND1 A:HIS442 4.0 24.6 1.0
N A:GLY356 4.2 29.9 1.0
S1A A:CFM496 4.2 31.2 1.0
CE1 A:HIS442 4.2 22.9 1.0
S4A A:CFM496 4.3 30.6 1.0
CA A:GLY356 4.4 27.5 1.0
NE A:ARG359 4.6 25.2 1.0
S5 A:CFM496 4.6 27.4 1.0
O7 A:HCA494 4.7 29.4 1.0
N A:GLY357 4.7 26.6 1.0
S2B A:CFM496 4.7 30.2 1.0
CG A:HIS442 4.7 20.9 1.0
CZ A:PHE381 4.7 26.9 1.0
O5 A:HCA494 4.7 25.9 1.0
CD A:ARG359 4.9 27.6 1.0
CB A:ILE355 5.0 28.4 1.0
CZ A:ARG359 5.0 28.2 1.0
NE2 A:HIS442 5.0 22.1 1.0
FE1 A:CFM496 5.0 32.6 1.0

Iron binding site 6 out of 30 in 1fp4

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Iron binding site 6 out of 30 in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe496

b:28.0
occ:1.00
FE6 A:CFM496 0.0 28.0 1.0
S3B A:CFM496 2.3 22.9 1.0
S1B A:CFM496 2.3 27.4 1.0
S2B A:CFM496 2.3 30.2 1.0
FE2 A:CFM496 2.5 28.2 1.0
FE7 A:CFM496 2.6 28.5 1.0
FE5 A:CFM496 2.7 26.6 1.0
MO1 A:CFM496 2.8 27.8 1.0
FE3 A:CFM496 3.7 29.4 1.0
FE4 A:CFM496 3.7 30.0 1.0
O7 A:HCA494 3.8 29.4 1.0
CZ A:PHE381 3.8 26.9 1.0
S4B A:CFM496 3.9 25.4 1.0
S1A A:CFM496 4.2 31.2 1.0
S2A A:CFM496 4.3 28.2 1.0
CE2 A:PHE381 4.3 24.7 1.0
NH2 A:ARG96 4.4 28.8 1.0
O5 A:HCA494 4.4 25.9 1.0
S5 A:CFM496 4.6 27.4 1.0
CG1 A:VAL70 4.6 26.4 1.0
S3A A:CFM496 4.6 29.2 1.0
O1 A:HCA494 4.7 32.8 1.0
C3 A:HCA494 4.8 32.3 1.0
ND1 A:HIS442 4.8 24.6 1.0
CE1 A:PHE381 4.9 30.9 1.0
FE1 A:CFM496 4.9 32.6 1.0
C2 A:HCA494 5.0 32.1 1.0

Iron binding site 7 out of 30 in 1fp4

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Iron binding site 7 out of 30 in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe496

b:28.5
occ:1.00
FE7 A:CFM496 0.0 28.5 1.0
S5 A:CFM496 2.3 27.4 1.0
S4B A:CFM496 2.3 25.4 1.0
S3B A:CFM496 2.3 22.9 1.0
FE3 A:CFM496 2.5 29.4 1.0
FE6 A:CFM496 2.6 28.0 1.0
FE5 A:CFM496 2.7 26.6 1.0
MO1 A:CFM496 2.8 27.8 1.0
NH2 A:ARG96 3.3 28.8 1.0
O5 A:HCA494 3.6 25.9 1.0
FE2 A:CFM496 3.6 28.2 1.0
FE4 A:CFM496 3.7 30.0 1.0
S1B A:CFM496 3.8 27.4 1.0
S2A A:CFM496 4.2 28.2 1.0
S4A A:CFM496 4.3 30.6 1.0
CD A:ARG96 4.5 28.1 1.0
CZ A:ARG96 4.5 27.7 1.0
S2B A:CFM496 4.5 30.2 1.0
NH1 A:ARG359 4.6 29.8 1.0
CZ A:ARG359 4.6 28.2 1.0
O7 A:HCA494 4.6 29.4 1.0
S3A A:CFM496 4.6 29.2 1.0
ND1 A:HIS442 4.8 24.6 1.0
C7 A:HCA494 4.8 30.3 1.0
FE1 A:CFM496 4.9 32.6 1.0
NH2 A:ARG359 5.0 32.3 1.0
NE A:ARG359 5.0 25.2 1.0
NE A:ARG96 5.0 31.4 1.0

Iron binding site 8 out of 30 in 1fp4

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Iron binding site 8 out of 30 in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe498

b:31.5
occ:1.00
FE1 A:CLP498 0.0 31.5 1.0
SG B:CYS95 2.3 20.5 1.0
S2A A:CLP498 2.3 29.6 1.0
S1A A:CLP498 2.3 28.5 1.0
S4A A:CLP498 2.3 23.1 1.0
FE2 A:CLP498 2.6 33.7 1.0
FE3 A:CLP498 2.7 28.1 1.0
FE4 A:CLP498 2.8 30.1 1.0
FE8 A:CLP498 3.0 23.8 1.0
N B:CYS95 3.3 17.0 1.0
CB B:CYS95 3.6 21.9 1.0
CA B:CYS95 3.6 20.2 1.0
S3A A:CLP498 3.8 29.7 1.0
S4B A:CLP498 4.0 21.7 1.0
C B:GLY94 4.1 20.0 1.0
CB B:SER92 4.1 29.0 1.0
O B:HOH542 4.2 25.1 1.0
SG A:CYS154 4.4 31.5 1.0
CA B:GLY94 4.5 18.7 1.0
SG A:CYS88 4.6 20.6 1.0
SG A:CYS62 4.8 34.0 1.0
OG B:SER92 4.8 34.2 1.0
FE5 A:CLP498 4.8 28.2 1.0
N B:GLY94 4.8 25.4 1.0
O B:GLY94 4.9 25.6 1.0

Iron binding site 9 out of 30 in 1fp4

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Iron binding site 9 out of 30 in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe498

b:33.7
occ:1.00
FE2 A:CLP498 0.0 33.7 1.0
S2A A:CLP498 2.3 29.6 1.0
SG A:CYS154 2.3 31.5 1.0
S3A A:CLP498 2.3 29.7 1.0
S1A A:CLP498 2.3 28.5 1.0
FE1 A:CLP498 2.6 31.5 1.0
FE3 A:CLP498 2.7 28.1 1.0
FE4 A:CLP498 2.8 30.1 1.0
CA A:GLY185 3.4 35.5 1.0
N A:GLY185 3.7 34.7 1.0
N A:CYS154 3.8 33.2 1.0
CB A:CYS154 3.9 34.5 1.0
S4A A:CLP498 3.9 23.1 1.0
O B:HOH542 3.9 25.1 1.0
OG B:SER92 4.2 34.2 1.0
C A:GLY185 4.2 35.3 1.0
CB B:SER92 4.3 29.0 1.0
CA A:CYS154 4.3 35.4 1.0
SG B:CYS95 4.5 20.5 1.0
N A:PHE186 4.6 34.6 1.0
FE8 A:CLP498 4.7 23.8 1.0
SG A:CYS62 4.7 34.0 1.0
C A:GLU153 4.9 29.2 1.0
O A:GLY185 4.9 37.1 1.0
C A:GLU184 5.0 35.3 1.0
CB A:CYS62 5.0 29.5 1.0

Iron binding site 10 out of 30 in 1fp4

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Iron binding site 10 out of 30 in the Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Crystal Structure of the Alpha-H195Q Mutant of Nitrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe498

b:28.1
occ:1.00
FE3 A:CLP498 0.0 28.1 1.0
S2A A:CLP498 2.3 29.6 1.0
SG A:CYS62 2.3 34.0 1.0
S4A A:CLP498 2.3 23.1 1.0
S3A A:CLP498 2.3 29.7 1.0
FE4 A:CLP498 2.7 30.1 1.0
FE1 A:CLP498 2.7 31.5 1.0
FE2 A:CLP498 2.7 33.7 1.0
CB A:CYS62 3.3 29.5 1.0
S1A A:CLP498 3.9 28.5 1.0
CA A:GLY185 3.9 35.5 1.0
CB A:TYR64 3.9 32.4 1.0
CA B:GLY94 4.2 18.7 1.0
C B:GLY94 4.4 20.0 1.0
CD2 A:TYR64 4.4 32.1 1.0
N B:CYS95 4.4 17.0 1.0
CG A:TYR64 4.5 31.7 1.0
N A:GLY185 4.5 34.7 1.0
CE1 B:TYR98 4.7 27.6 1.0
CA A:CYS62 4.7 32.7 1.0
SG A:CYS88 4.8 20.6 1.0
SG B:CYS95 4.9 20.5 1.0
CD1 B:TYR98 4.9 22.6 1.0
N B:GLY94 4.9 25.4 1.0
C A:GLY185 4.9 35.3 1.0
N A:TYR64 5.0 32.1 1.0

Reference:

M.Sorlie, J.Christiansen, B.J.Lemon, J.W.Peters, D.R.Dean, B.J.Hales. Mechanistic Features and Structure of the Nitrogenase Alpha-GLN195 Mofe Protein Biochemistry V. 40 1540 2001.
ISSN: ISSN 0006-2960
PubMed: 11327812
DOI: 10.1021/BI0013997
Page generated: Sat Aug 3 05:11:21 2024

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