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Iron in PDB 3e4y: Crystal Structure of A 33KDA Catalase-Related Protein From Mycobacterium Avium Subsp. Paratuberculosis. I2(1)2(1)2(1) Crystal Form

Protein crystallography data

The structure of Crystal Structure of A 33KDA Catalase-Related Protein From Mycobacterium Avium Subsp. Paratuberculosis. I2(1)2(1)2(1) Crystal Form, PDB code: 3e4y was solved by S.Pakhomova, M.E.Newcomer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.20 / 2.60
Space group I 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 69.604, 92.680, 165.499, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 25.7

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of A 33KDA Catalase-Related Protein From Mycobacterium Avium Subsp. Paratuberculosis. I2(1)2(1)2(1) Crystal Form (pdb code 3e4y). 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 Crystal Structure of A 33KDA Catalase-Related Protein From Mycobacterium Avium Subsp. Paratuberculosis. I2(1)2(1)2(1) Crystal Form, PDB code: 3e4y:

Iron binding site 1 out of 1 in 3e4y

Go back to Iron Binding Sites List in 3e4y
Iron binding site 1 out of 1 in the Crystal Structure of A 33KDA Catalase-Related Protein From Mycobacterium Avium Subsp. Paratuberculosis. I2(1)2(1)2(1) Crystal Form


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 A 33KDA Catalase-Related Protein From Mycobacterium Avium Subsp. Paratuberculosis. I2(1)2(1)2(1) Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:59.0
occ:1.00
FE A:HEM501 0.0 59.0 1.0
NC A:HEM501 2.0 49.2 1.0
NA A:HEM501 2.0 48.9 1.0
ND A:HEM501 2.0 49.4 1.0
NB A:HEM501 2.0 51.8 1.0
OH A:TYR294 2.5 34.3 1.0
C1D A:HEM501 3.0 46.3 1.0
C1C A:HEM501 3.0 44.8 1.0
C4C A:HEM501 3.0 47.2 1.0
C4B A:HEM501 3.0 40.8 1.0
C4D A:HEM501 3.0 41.5 1.0
C1A A:HEM501 3.0 45.0 1.0
C1B A:HEM501 3.0 45.9 1.0
C4A A:HEM501 3.1 45.4 1.0
CHD A:HEM501 3.4 45.8 1.0
CHC A:HEM501 3.4 45.8 1.0
CHA A:HEM501 3.4 44.0 1.0
CHB A:HEM501 3.4 46.9 1.0
CZ A:TYR294 3.5 40.6 1.0
CE2 A:TYR294 3.8 41.5 1.0
NH1 A:ARG290 4.0 23.1 1.0
CD A:ARG290 4.1 33.3 1.0
C2C A:HEM501 4.2 41.5 1.0
C3C A:HEM501 4.3 42.3 1.0
C2A A:HEM501 4.3 38.9 1.0
C3A A:HEM501 4.3 43.0 1.0
C2D A:HEM501 4.3 39.7 1.0
C2B A:HEM501 4.3 40.7 1.0
C3D A:HEM501 4.3 37.3 1.0
C3B A:HEM501 4.3 37.9 1.0
O3 A:GOL610 4.4 35.9 1.0
CD2 A:HIS28 4.6 35.2 1.0
CE1 A:TYR294 4.6 36.6 1.0
NE2 A:HIS28 4.7 30.8 1.0
CZ A:ARG290 4.7 37.4 1.0
NE A:ARG290 4.8 31.8 1.0
O2 A:GOL610 4.8 51.8 1.0

Reference:

S.Pakhomova, B.Gao, W.E.Boeglin, A.R.Brash, M.E.Newcomer. The Structure and Peroxidase Activity of A 33-kDa Catalase-Related Protein From Mycobacterium Avium Ssp. Paratuberculosis. Protein Sci. V. 18 2559 2009.
ISSN: ISSN 0961-8368
PubMed: 19827095
DOI: 10.1002/PRO.265
Page generated: Sun Aug 4 09:21:16 2024

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