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Iron in PDB 4e2p: Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis

Protein crystallography data

The structure of Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis, PDB code: 4e2p was solved by H.D.Zhang, J.Chen, H.Wang, L.Huang, H.J.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.38 / 2.36
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.140, 72.290, 103.290, 90.00, 90.00, 90.00
R / Rfree (%) 23.9 / 28

Other elements in 4e2p:

The structure of Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis (pdb code 4e2p). 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 Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis, PDB code: 4e2p:

Iron binding site 1 out of 1 in 4e2p

Go back to Iron Binding Sites List in 4e2p
Iron binding site 1 out of 1 in the Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis


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 Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:12.6
occ:1.00
FE A:HEM401 0.0 12.6 1.0
NC A:HEM401 2.0 12.6 1.0
NA A:HEM401 2.0 12.4 1.0
ND A:HEM401 2.1 12.6 1.0
NB A:HEM401 2.1 12.5 1.0
SG A:CYS346 2.2 13.5 1.0
O A:HOH686 2.4 12.6 1.0
C1C A:HEM401 2.9 12.6 1.0
C4C A:HEM401 3.0 12.6 1.0
C1A A:HEM401 3.0 12.4 1.0
C4A A:HEM401 3.1 12.3 1.0
C4B A:HEM401 3.1 12.5 1.0
C4D A:HEM401 3.2 12.5 1.0
C1D A:HEM401 3.2 12.6 1.0
C1B A:HEM401 3.2 12.4 1.0
CB A:CYS346 3.3 13.5 1.0
CHC A:HEM401 3.4 12.5 1.0
CHA A:HEM401 3.4 12.4 1.0
CHD A:HEM401 3.5 12.6 1.0
CHB A:HEM401 3.6 12.4 1.0
CA A:CYS346 4.0 13.7 1.0
C3C A:HEM401 4.1 12.6 1.0
C2C A:HEM401 4.1 12.6 1.0
O A:ALA236 4.2 14.4 1.0
C2A A:HEM401 4.2 12.3 1.0
C3A A:HEM401 4.3 12.3 1.0
C3B A:HEM401 4.5 12.4 1.0
C2D A:HEM401 4.5 12.7 1.0
C3D A:HEM401 4.5 12.6 1.0
C2B A:HEM401 4.6 12.4 1.0
N A:GLY348 4.6 14.2 1.0
O A:HOH501 4.6 30.0 1.0
C A:CYS346 4.7 13.9 1.0
N A:LEU347 4.8 14.1 1.0
CD1 A:PHE339 4.9 12.5 1.0
CA A:GLY348 4.9 14.3 1.0
O A:HOH502 4.9 30.0 1.0
CB A:ALA236 5.0 14.8 1.0

Reference:

H.D.Zhang, J.Chen, H.Wang, L.Huang, H.J.Zhang. Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis To Be Published.
Page generated: Mon Aug 5 01:29:57 2024

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