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Iron in PDB 1sy7: Crystal Structure of the Catalase-1 From Neurospora Crassa, Native Structure at 1.75A Resolution.

Enzymatic activity of Crystal Structure of the Catalase-1 From Neurospora Crassa, Native Structure at 1.75A Resolution.

All present enzymatic activity of Crystal Structure of the Catalase-1 From Neurospora Crassa, Native Structure at 1.75A Resolution.:
1.11.1.6;

Protein crystallography data

The structure of Crystal Structure of the Catalase-1 From Neurospora Crassa, Native Structure at 1.75A Resolution., PDB code: 1sy7 was solved by A.Diaz, E.Horjales, E.Rudino-Pinera, R.Arreola, W.Hansberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.75
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 130.007, 182.242, 90.364, 90.00, 133.41, 90.00
R / Rfree (%) 18.3 / 20.6

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Catalase-1 From Neurospora Crassa, Native Structure at 1.75A Resolution. (pdb code 1sy7). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of the Catalase-1 From Neurospora Crassa, Native Structure at 1.75A Resolution., PDB code: 1sy7:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1sy7

Go back to Iron Binding Sites List in 1sy7
Iron binding site 1 out of 4 in the Crystal Structure of the Catalase-1 From Neurospora Crassa, Native Structure at 1.75A 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 the Catalase-1 From Neurospora Crassa, Native Structure at 1.75A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1880

b:14.6
occ:0.43
FE A:HDD1880 0.0 14.6 0.4
FE A:HEM1883 0.2 18.5 0.6
NC A:HDD1880 2.0 15.8 0.4
NB A:HEM1883 2.0 18.9 0.6
NA A:HDD1880 2.1 16.1 0.4
NA A:HEM1883 2.1 18.2 0.6
NB A:HDD1880 2.1 16.1 0.4
ND A:HDD1880 2.1 15.8 0.4
NC A:HEM1883 2.2 18.7 0.6
OH A:TYR379 2.4 17.8 1.0
ND A:HEM1883 2.4 17.9 0.6
C4C A:HDD1880 3.0 6.7 0.4
C1D A:HDD1880 3.0 7.0 0.4
C1B A:HEM1883 3.0 13.0 0.6
C4B A:HEM1883 3.0 15.1 0.6
C1C A:HDD1880 3.0 7.2 0.4
C4A A:HEM1883 3.1 11.5 0.6
C4B A:HDD1880 3.1 7.0 0.4
C4A A:HDD1880 3.1 6.2 0.4
C1A A:HDD1880 3.1 7.4 0.4
C1B A:HDD1880 3.1 6.6 0.4
C1C A:HEM1883 3.1 13.9 0.6
C4C A:HEM1883 3.2 13.3 0.6
C1A A:HEM1883 3.2 13.0 0.6
C4D A:HDD1880 3.2 7.8 0.4
CZ A:TYR379 3.3 14.1 1.0
C1D A:HEM1883 3.3 11.2 0.6
CHD A:HDD1880 3.4 7.2 0.4
CHB A:HEM1883 3.4 12.7 0.6
CHC A:HDD1880 3.5 6.3 0.4
C4D A:HEM1883 3.5 12.8 0.6
CHC A:HEM1883 3.5 15.5 0.6
CHA A:HDD1880 3.5 7.0 0.4
CHB A:HDD1880 3.5 6.5 0.4
CHD A:HEM1883 3.6 13.6 0.6
CE2 A:TYR379 3.6 11.9 1.0
CHA A:HEM1883 3.6 12.2 0.6
NH2 A:ARG375 4.1 12.1 1.0
C3C A:HDD1880 4.2 6.8 0.4
NE A:ARG375 4.2 13.8 1.0
C3B A:HEM1883 4.3 14.5 0.6
C2C A:HDD1880 4.3 6.2 0.4
C2B A:HEM1883 4.3 13.4 0.6
C2D A:HDD1880 4.3 6.8 0.4
C3B A:HDD1880 4.3 5.7 0.4
CE1 A:TYR379 4.4 13.8 1.0
C2A A:HDD1880 4.4 5.7 0.4
C3A A:HEM1883 4.4 11.3 0.6
C3A A:HDD1880 4.4 6.2 0.4
C2B A:HDD1880 4.4 6.2 0.4
C2A A:HEM1883 4.4 10.7 0.6
C3C A:HEM1883 4.4 14.0 0.6
C2C A:HEM1883 4.4 13.7 0.6
C3D A:HDD1880 4.4 7.7 0.4
O A:HOH2427 4.5 19.0 1.0
CZ A:PHE178 4.5 14.6 1.0
CZ A:ARG375 4.5 15.2 1.0
C2D A:HEM1883 4.6 12.8 0.6
C3D A:HEM1883 4.7 14.2 0.6
CG2 A:VAL91 4.8 11.4 1.0
NE2 A:HIS92 4.8 13.5 1.0
CD2 A:HIS92 4.9 12.6 1.0
CE2 A:PHE178 4.9 13.7 1.0
CD2 A:TYR379 4.9 12.3 1.0

Iron binding site 2 out of 4 in 1sy7

Go back to Iron Binding Sites List in 1sy7
Iron binding site 2 out of 4 in the Crystal Structure of the Catalase-1 From Neurospora Crassa, Native Structure at 1.75A 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 the Catalase-1 From Neurospora Crassa, Native Structure at 1.75A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1883

b:18.5
occ:0.57
FE A:HEM1883 0.0 18.5 0.6
FE A:HDD1880 0.2 14.6 0.4
ND A:HDD1880 2.0 15.8 0.4
NC A:HDD1880 2.0 15.8 0.4
NA A:HDD1880 2.1 16.1 0.4
NA A:HEM1883 2.1 18.2 0.6
NC A:HEM1883 2.2 18.7 0.6
NB A:HEM1883 2.2 18.9 0.6
ND A:HEM1883 2.2 17.9 0.6
NB A:HDD1880 2.3 16.1 0.4
OH A:TYR379 2.3 17.8 1.0
C1D A:HDD1880 2.9 7.0 0.4
C4C A:HDD1880 2.9 6.7 0.4
C4C A:HEM1883 3.1 13.3 0.6
C1C A:HDD1880 3.1 7.2 0.4
C4D A:HDD1880 3.1 7.8 0.4
C1A A:HDD1880 3.1 7.4 0.4
CZ A:TYR379 3.1 14.1 1.0
C1D A:HEM1883 3.1 11.2 0.6
C4A A:HEM1883 3.1 11.5 0.6
C4B A:HEM1883 3.2 15.1 0.6
C1B A:HEM1883 3.2 13.0 0.6
C1A A:HEM1883 3.2 13.0 0.6
C1C A:HEM1883 3.2 13.9 0.6
C4A A:HDD1880 3.2 6.2 0.4
C4B A:HDD1880 3.2 7.0 0.4
CHD A:HDD1880 3.3 7.2 0.4
C1B A:HDD1880 3.3 6.6 0.4
C4D A:HEM1883 3.4 12.8 0.6
CHA A:HDD1880 3.4 7.0 0.4
CE2 A:TYR379 3.5 11.9 1.0
CHD A:HEM1883 3.5 13.6 0.6
CHA A:HEM1883 3.5 12.2 0.6
CHB A:HEM1883 3.6 12.7 0.6
CHC A:HEM1883 3.6 15.5 0.6
CHC A:HDD1880 3.6 6.3 0.4
CHB A:HDD1880 3.7 6.5 0.4
NH2 A:ARG375 4.1 12.1 1.0
C2D A:HDD1880 4.2 6.8 0.4
C3C A:HDD1880 4.2 6.8 0.4
CE1 A:TYR379 4.2 13.8 1.0
NE A:ARG375 4.2 13.8 1.0
C2C A:HDD1880 4.3 6.2 0.4
C3D A:HDD1880 4.3 7.7 0.4
C3C A:HEM1883 4.4 14.0 0.6
C2A A:HDD1880 4.4 5.7 0.4
C3B A:HEM1883 4.4 14.5 0.6
C2A A:HEM1883 4.4 10.7 0.6
C3A A:HEM1883 4.4 11.3 0.6
C2C A:HEM1883 4.4 13.7 0.6
C2D A:HEM1883 4.4 12.8 0.6
C3A A:HDD1880 4.5 6.2 0.4
C2B A:HEM1883 4.5 13.4 0.6
C3B A:HDD1880 4.5 5.7 0.4
C3D A:HEM1883 4.5 14.2 0.6
CZ A:PHE178 4.6 14.6 1.0
C2B A:HDD1880 4.6 6.2 0.4
CZ A:ARG375 4.6 15.2 1.0
O A:HOH2427 4.6 19.0 1.0
CD2 A:TYR379 4.7 12.3 1.0
CG2 A:VAL91 4.8 11.4 1.0
NE2 A:HIS92 4.9 13.5 1.0
CE2 A:PHE178 4.9 13.7 1.0
CD2 A:HIS92 4.9 12.6 1.0

Iron binding site 3 out of 4 in 1sy7

Go back to Iron Binding Sites List in 1sy7
Iron binding site 3 out of 4 in the Crystal Structure of the Catalase-1 From Neurospora Crassa, Native Structure at 1.75A Resolution.


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 Catalase-1 From Neurospora Crassa, Native Structure at 1.75A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1881

b:15.7
occ:0.43
FE B:HDD1881 0.0 15.7 0.4
FE B:HEM1882 0.2 19.4 0.6
NC B:HDD1881 2.0 15.9 0.4
NB B:HEM1882 2.0 19.1 0.6
NA B:HDD1881 2.1 16.1 0.4
NA B:HEM1882 2.1 18.3 0.6
NB B:HDD1881 2.1 16.2 0.4
ND B:HDD1881 2.1 16.0 0.4
NC B:HEM1882 2.2 18.6 0.6
OH B:TYR379 2.4 17.0 1.0
ND B:HEM1882 2.4 18.2 0.6
C4C B:HDD1881 3.0 6.9 0.4
C1D B:HDD1881 3.0 7.4 0.4
C4B B:HEM1882 3.0 15.1 0.6
C1B B:HEM1882 3.0 13.2 0.6
C1C B:HDD1881 3.0 7.0 0.4
C4A B:HEM1882 3.1 11.5 0.6
C4B B:HDD1881 3.1 6.8 0.4
C4A B:HDD1881 3.1 6.2 0.4
C1C B:HEM1882 3.1 13.7 0.6
C1A B:HDD1881 3.1 7.8 0.4
C1B B:HDD1881 3.1 6.8 0.4
C4C B:HEM1882 3.2 13.6 0.6
C1A B:HEM1882 3.2 13.3 0.6
C4D B:HDD1881 3.2 8.0 0.4
CZ B:TYR379 3.3 14.5 1.0
C1D B:HEM1882 3.3 11.7 0.6
CHD B:HDD1881 3.4 6.8 0.4
CHB B:HEM1882 3.4 12.7 0.6
CHC B:HDD1881 3.5 6.2 0.4
CHC B:HEM1882 3.5 15.3 0.6
C4D B:HEM1882 3.5 13.1 0.6
CHA B:HDD1881 3.5 7.0 0.4
CHB B:HDD1881 3.5 6.6 0.4
CHD B:HEM1882 3.6 13.2 0.6
CE2 B:TYR379 3.6 12.1 1.0
CHA B:HEM1882 3.6 12.2 0.6
NH2 B:ARG375 4.1 12.2 1.0
NE B:ARG375 4.2 14.3 1.0
C3C B:HDD1881 4.2 6.6 0.4
C3B B:HEM1882 4.2 14.6 0.6
C2C B:HDD1881 4.3 6.3 0.4
C2B B:HEM1882 4.3 13.3 0.6
C3B B:HDD1881 4.3 5.8 0.4
C2D B:HDD1881 4.3 6.8 0.4
CE1 B:TYR379 4.4 13.2 1.0
C2A B:HDD1881 4.4 5.7 0.4
C3A B:HEM1882 4.4 11.2 0.6
C3A B:HDD1881 4.4 6.2 0.4
C2B B:HDD1881 4.4 6.0 0.4
C3C B:HEM1882 4.4 13.6 0.6
C2A B:HEM1882 4.4 10.8 0.6
C2C B:HEM1882 4.4 13.7 0.6
C3D B:HDD1881 4.4 7.5 0.4
CZ B:PHE178 4.5 14.6 1.0
CZ B:ARG375 4.5 14.7 1.0
C2D B:HEM1882 4.6 12.8 0.6
O B:HOH2001 4.6 21.8 1.0
C3D B:HEM1882 4.7 14.2 0.6
NE2 B:HIS92 4.8 13.1 1.0
CG2 B:VAL91 4.8 11.4 1.0
CD2 B:HIS92 4.9 12.6 1.0
CD2 B:TYR379 4.9 12.5 1.0
CE2 B:PHE178 4.9 14.0 1.0

Iron binding site 4 out of 4 in 1sy7

Go back to Iron Binding Sites List in 1sy7
Iron binding site 4 out of 4 in the Crystal Structure of the Catalase-1 From Neurospora Crassa, Native Structure at 1.75A Resolution.


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 Catalase-1 From Neurospora Crassa, Native Structure at 1.75A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1882

b:19.4
occ:0.57
FE B:HEM1882 0.0 19.4 0.6
FE B:HDD1881 0.2 15.7 0.4
ND B:HDD1881 2.0 16.0 0.4
NC B:HDD1881 2.0 15.9 0.4
NA B:HDD1881 2.1 16.1 0.4
NA B:HEM1882 2.1 18.3 0.6
NC B:HEM1882 2.2 18.6 0.6
NB B:HEM1882 2.2 19.1 0.6
ND B:HEM1882 2.2 18.2 0.6
NB B:HDD1881 2.3 16.2 0.4
OH B:TYR379 2.3 17.0 1.0
C1D B:HDD1881 2.9 7.4 0.4
C4C B:HDD1881 2.9 6.9 0.4
C4C B:HEM1882 3.1 13.6 0.6
C1A B:HDD1881 3.1 7.8 0.4
C1C B:HDD1881 3.1 7.0 0.4
C4D B:HDD1881 3.1 8.0 0.4
CZ B:TYR379 3.1 14.5 1.0
C1D B:HEM1882 3.1 11.7 0.6
C4A B:HEM1882 3.1 11.5 0.6
C4B B:HEM1882 3.2 15.1 0.6
C1A B:HEM1882 3.2 13.3 0.6
C1C B:HEM1882 3.2 13.7 0.6
C1B B:HEM1882 3.2 13.2 0.6
C4A B:HDD1881 3.2 6.2 0.4
C4B B:HDD1881 3.2 6.8 0.4
CHD B:HDD1881 3.3 6.8 0.4
C1B B:HDD1881 3.3 6.8 0.4
C4D B:HEM1882 3.4 13.1 0.6
CHA B:HDD1881 3.4 7.0 0.4
CE2 B:TYR379 3.5 12.1 1.0
CHD B:HEM1882 3.5 13.2 0.6
CHA B:HEM1882 3.5 12.2 0.6
CHB B:HEM1882 3.6 12.7 0.6
CHC B:HEM1882 3.6 15.3 0.6
CHC B:HDD1881 3.6 6.2 0.4
CHB B:HDD1881 3.7 6.6 0.4
NH2 B:ARG375 4.1 12.2 1.0
C2D B:HDD1881 4.2 6.8 0.4
C3C B:HDD1881 4.2 6.6 0.4
CE1 B:TYR379 4.2 13.2 1.0
NE B:ARG375 4.2 14.3 1.0
C2C B:HDD1881 4.3 6.3 0.4
C3D B:HDD1881 4.3 7.5 0.4
C2A B:HDD1881 4.4 5.7 0.4
C3C B:HEM1882 4.4 13.6 0.6
C3B B:HEM1882 4.4 14.6 0.6
C2A B:HEM1882 4.4 10.8 0.6
C3A B:HEM1882 4.4 11.2 0.6
C2C B:HEM1882 4.4 13.7 0.6
C2D B:HEM1882 4.4 12.8 0.6
C3A B:HDD1881 4.4 6.2 0.4
C2B B:HEM1882 4.5 13.3 0.6
C3B B:HDD1881 4.5 5.8 0.4
C3D B:HEM1882 4.5 14.2 0.6
CZ B:PHE178 4.6 14.6 1.0
C2B B:HDD1881 4.6 6.0 0.4
CZ B:ARG375 4.6 14.7 1.0
CD2 B:TYR379 4.7 12.5 1.0
CG2 B:VAL91 4.8 11.4 1.0
O B:HOH2001 4.8 21.8 1.0
NE2 B:HIS92 4.9 13.1 1.0
CE2 B:PHE178 4.9 14.0 1.0
CD2 B:HIS92 4.9 12.6 1.0

Reference:

A.Diaz, E.Horjales, E.Rudino-Pinera, R.Arreola, W.Hansberg. Unusual Cys-Tyr Covalent Bond in A Large Catalase J.Mol.Biol. V. 342 971 2004.
ISSN: ISSN 0022-2836
PubMed: 15342250
DOI: 10.1016/J.JMB.2004.07.027
Page generated: Sun Dec 13 14:32:15 2020

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