Iron in PDB 5i0r: D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8

Enzymatic activity of D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8

All present enzymatic activity of D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8:
1.13.11.20;

Protein crystallography data

The structure of D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8, PDB code: 5i0r was solved by K.M.Kean, C.M.Driggers, P.A.Karplus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.94 / 1.35
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 57.600, 57.600, 122.400, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 20

Other elements in 5i0r:

The structure of D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8 also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8 (pdb code 5i0r). 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 D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8, PDB code: 5i0r:

Iron binding site 1 out of 1 in 5i0r

Go back to Iron Binding Sites List in 5i0r
Iron binding site 1 out of 1 in the D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of D-Cysteine Bound C93A Mutant of Cysteine Dioxygenase at pH 8 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:11.2
occ:1.00
H2 A:DCY502 1.7 15.7 0.5
H2 A:DCY502 1.8 17.5 0.1
N A:DCY502 2.0 13.1 0.5
NE2 A:HIS140 2.0 11.3 1.0
NE2 A:HIS88 2.0 12.1 1.0
N A:DCY502 2.1 14.6 0.1
NE2 A:HIS86 2.1 11.5 0.5
SG A:DCY502 2.2 16.7 0.5
CL A:CL503 2.3 15.0 0.5
HG A:DCY502 2.4 14.0 0.1
SG A:DCY502 2.6 11.7 0.1
H A:DCY502 2.7 15.7 0.5
H A:DCY502 2.8 17.5 0.1
CE1 A:HIS88 2.9 10.3 1.0
CE1 A:HIS140 3.0 10.8 1.0
CA A:DCY502 3.0 13.4 0.5
CA A:DCY502 3.0 8.4 0.1
CD2 A:HIS86 3.0 9.9 0.5
CD2 A:HIS140 3.1 10.6 1.0
HE1 A:HIS88 3.1 12.3 1.0
CD2 A:HIS88 3.1 12.0 1.0
HG A:DCY502 3.1 20.1 0.5
HD2 A:HIS86 3.1 11.9 0.5
CB A:DCY502 3.1 18.4 0.5
HE1 A:HIS140 3.1 12.9 1.0
CB A:DCY502 3.2 15.9 0.1
CE1 A:HIS86 3.2 9.9 0.5
HB2 A:DCY502 3.3 19.1 0.1
HA A:DCY502 3.3 10.0 0.1
HD2 A:HIS140 3.3 12.8 1.0
HA A:DCY502 3.3 16.1 0.5
HD2 A:HIS88 3.3 14.3 1.0
HB2 A:DCY502 3.4 22.1 0.5
HE1 A:HIS86 3.4 11.8 0.5
O A:HOH667 3.7 24.3 0.6
HH A:TYR157 3.9 18.6 1.0
HB3 A:DCY502 4.0 22.1 0.5
O A:HOH746 4.1 23.0 1.0
ND1 A:HIS88 4.1 11.1 1.0
HB3 A:DCY502 4.1 19.1 0.1
ND1 A:HIS140 4.1 12.1 1.0
HG21 A:ILE133 4.1 14.8 1.0
CG A:HIS140 4.2 11.0 1.0
CG A:HIS88 4.2 10.8 1.0
CG A:HIS86 4.2 10.6 0.5
HG21 A:VAL142 4.2 17.3 1.0
HB2 A:HIS86 4.3 17.1 0.6
ND1 A:HIS86 4.3 7.2 0.5
HE1 A:TYR157 4.3 17.9 1.0
HG23 A:VAL142 4.3 17.3 1.0
C A:DCY502 4.3 16.3 0.5
C A:DCY502 4.4 20.1 0.1
O A:DCY502 4.6 13.6 0.5
HB3 A:HIS86 4.7 17.1 0.6
HG22 A:ILE133 4.7 14.8 1.0
O A:DCY502 4.7 21.4 0.1
CG2 A:VAL142 4.7 14.4 1.0
OH A:TYR157 4.8 15.5 1.0
CG2 A:ILE133 4.8 12.4 1.0
HD12 A:LEU95 4.8 21.2 1.0
O A:HOH793 4.8 21.4 1.0
HD1 A:HIS88 4.9 13.3 1.0
O A:HOH685 4.9 28.0 1.0
HD1 A:HIS140 4.9 14.5 1.0
HG23 A:ILE133 4.9 14.8 1.0
CB A:HIS86 4.9 14.2 0.6

Reference:

C.M.Driggers, K.M.Kean, L.L.Hirschberger, R.B.Cooley, M.H.Stipanuk, P.A.Karplus. Structure-Based Insights Into the Role of the Cys-Tyr Crosslink and Inhibitor Recognition By Mammalian Cysteine Dioxygenase. J. Mol. Biol. V. 428 3999 2016.
ISSN: ESSN 1089-8638
PubMed: 27477048
DOI: 10.1016/J.JMB.2016.07.012
Page generated: Sun Dec 13 16:03:27 2020

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