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Iron in PDB 5xnf: Crystal Structure of the Branched-Chain Polyamine Synthase (Bpsa) From Thermococcus Kodakarensis

Enzymatic activity of Crystal Structure of the Branched-Chain Polyamine Synthase (Bpsa) From Thermococcus Kodakarensis

All present enzymatic activity of Crystal Structure of the Branched-Chain Polyamine Synthase (Bpsa) From Thermococcus Kodakarensis:
2.5.1.128;

Protein crystallography data

The structure of Crystal Structure of the Branched-Chain Polyamine Synthase (Bpsa) From Thermococcus Kodakarensis, PDB code: 5xnf was solved by E.Mizohata, K.M.Tse, J.Fujita, T.Inoue, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 89.661, 105.167, 80.888, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / 24.4

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Branched-Chain Polyamine Synthase (Bpsa) From Thermococcus Kodakarensis (pdb code 5xnf). 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 the Branched-Chain Polyamine Synthase (Bpsa) From Thermococcus Kodakarensis, PDB code: 5xnf:

Iron binding site 1 out of 1 in 5xnf

Go back to Iron Binding Sites List in 5xnf
Iron binding site 1 out of 1 in the Crystal Structure of the Branched-Chain Polyamine Synthase (Bpsa) From Thermococcus Kodakarensis


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 Branched-Chain Polyamine Synthase (Bpsa) From Thermococcus Kodakarensis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:40.3
occ:0.80
 SG A:CYS91 2.2 42.1 1.0
SG B:CYS91 2.3 45.5 1.0
SG B:CYS94 2.3 49.4 1.0
SG A:CYS94 2.4 51.5 1.0
CB A:CYS91 3.1 40.6 1.0
CB B:CYS91 3.1 44.8 1.0
CB A:CYS94 3.3 44.4 1.0
CB B:CYS94 3.3 44.8 1.0
N A:CYS94 3.7 43.1 1.0
N B:CYS94 3.8 45.5 1.0
CA A:CYS94 4.1 41.0 1.0
CA B:CYS94 4.2 41.8 1.0
CA B:CYS91 4.5 40.6 1.0
CA A:CYS91 4.5 39.1 1.0
CB A:HIS93 4.7 55.2 1.0
C B:CYS91 4.8 40.2 1.0
C A:HIS93 4.8 47.8 1.0
O B:CYS91 4.8 37.9 1.0
C A:CYS94 4.8 38.1 1.0
C A:CYS91 4.9 38.9 1.0
O A:CYS91 4.9 37.5 1.0
C B:HIS93 4.9 47.9 1.0
N B:HIS93 4.9 47.8 1.0
C B:CYS94 4.9 41.6 1.0
CB B:HIS93 5.0 59.3 1.0
N A:HIS93 5.0 45.0 1.0

Reference:

R.Hidese, K.M.Tse, S.Kimura, E.Mizohata, J.Fujita, Y.Horai, N.Umezawa, T.Higuchi, M.Niitsu, T.Oshima, T.Imanaka, T.Inoue, S.Fujiwara. Active Site Geometry of A Novel Aminopropyltransferase For Biosynthesis of Hyperthermophile-Specific Branched-Chain Polyamine. Febs J. V. 284 3684 2017.
ISSN: ISSN 1742-4658
PubMed: 28881427
DOI: 10.1111/FEBS.14262
Page generated: Tue Aug 6 11:48:10 2024

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