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Iron in PDB 1lrm: Crystal Structure of Binary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase with Dihydrobiopterin (BH2)

Enzymatic activity of Crystal Structure of Binary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase with Dihydrobiopterin (BH2)

All present enzymatic activity of Crystal Structure of Binary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase with Dihydrobiopterin (BH2):
1.14.16.1;

Protein crystallography data

The structure of Crystal Structure of Binary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase with Dihydrobiopterin (BH2), PDB code: 1lrm was solved by O.A.Andersen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.10
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 66.588, 108.117, 124.168, 90.00, 90.00, 90.00
R / Rfree (%) 21.1 / 23.5

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Binary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase with Dihydrobiopterin (BH2) (pdb code 1lrm). 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 Binary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase with Dihydrobiopterin (BH2), PDB code: 1lrm:

Iron binding site 1 out of 1 in 1lrm

Go back to Iron Binding Sites List in 1lrm
Iron binding site 1 out of 1 in the Crystal Structure of Binary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase with Dihydrobiopterin (BH2)


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 Binary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase with Dihydrobiopterin (BH2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe428

b:25.1
occ:1.00
 OE2 A:GLU330 2.2 33.5 1.0
NE2 A:HIS285 2.2 19.1 1.0
O A:HOH1174 2.3 20.1 1.0
NE2 A:HIS290 2.3 22.3 1.0
O A:HOH1143 2.4 21.2 1.0
O A:HOH1145 2.5 39.6 1.0
CD2 A:HIS290 3.1 20.1 1.0
CD A:GLU330 3.1 29.8 1.0
CD2 A:HIS285 3.2 18.7 1.0
CE1 A:HIS285 3.2 21.1 1.0
OE1 A:GLU330 3.4 33.1 1.0
CE1 A:HIS290 3.4 19.3 1.0
O4 A:HBI429 3.7 40.0 1.0
O A:HOH1183 4.1 31.3 1.0
O A:HOH1155 4.1 42.2 1.0
OE2 A:GLU286 4.3 19.7 1.0
CG A:HIS290 4.3 22.2 1.0
CG A:HIS285 4.3 21.0 1.0
ND1 A:HIS285 4.3 22.7 1.0
CG A:GLU330 4.4 28.8 1.0
ND1 A:HIS290 4.4 21.8 1.0
CB A:ALA345 4.6 17.9 1.0
OH A:TYR325 4.7 24.3 1.0
CB A:PRO281 4.8 21.6 1.0

Reference:

O.A.Andersen, N/A. N/A N/A.
Page generated: Sat Aug 3 09:55:17 2024

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