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Zinc in PDB 1ld3: Crystal Structure of B. Subilis Ferrochelatase with Zn(2+) Bound at the Active Site.

Enzymatic activity of Crystal Structure of B. Subilis Ferrochelatase with Zn(2+) Bound at the Active Site.

All present enzymatic activity of Crystal Structure of B. Subilis Ferrochelatase with Zn(2+) Bound at the Active Site.:
4.99.1.1;

Protein crystallography data

The structure of Crystal Structure of B. Subilis Ferrochelatase with Zn(2+) Bound at the Active Site., PDB code: 1ld3 was solved by D.Lecerof, M.N.Fodje, R.A.Leon, U.Olsson, A.Hansson, E.Sigfridsson, U.Ryde, M.Hansson, S.Al-Karadaghi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.48 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.636, 49.876, 118.532, 90.00, 90.00, 90.00
R / Rfree (%) 21.7 / 27.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of B. Subilis Ferrochelatase with Zn(2+) Bound at the Active Site. (pdb code 1ld3). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of B. Subilis Ferrochelatase with Zn(2+) Bound at the Active Site., PDB code: 1ld3:

Zinc binding site 1 out of 1 in 1ld3

Go back to Zinc Binding Sites List in 1ld3
Zinc binding site 1 out of 1 in the Crystal Structure of B. Subilis Ferrochelatase with Zn(2+) Bound at the Active Site.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of B. Subilis Ferrochelatase with Zn(2+) Bound at the Active Site. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:25.8
occ:0.94
O A:HOH432 2.0 44.1 1.0
NE2 A:HIS183 2.1 21.8 1.0
OE1 A:GLU264 2.2 34.3 1.0
O A:HOH433 2.3 24.6 1.0
CE1 A:HIS183 2.8 19.1 1.0
CD2 A:HIS183 3.3 19.8 1.0
CD A:GLU264 3.4 32.0 1.0
O A:HOH435 3.4 17.3 1.0
O A:HOH436 3.5 42.7 1.0
O A:SER222 3.7 32.6 1.0
ND1 A:HIS183 4.1 27.3 1.0
OE2 A:GLU264 4.1 32.3 1.0
CB A:SER222 4.2 22.2 1.0
OH A:TYR13 4.3 37.6 1.0
CG A:HIS183 4.3 28.7 1.0
CG A:GLU264 4.4 29.8 1.0
C A:SER222 4.7 29.1 1.0
CZ A:TYR13 5.0 41.0 1.0

Reference:

D.Lecerof, M.N.Fodje, R.A.Leon, U.Olsson, A.Hansson, E.Sigfridsson, U.Ryde, M.Hansson, S.Al-Karadaghi. Metal Binding to Bacillus Subtilis Ferrochelatase and Interaction Between Metal Sites J.Biol.Inorg.Chem. V. 8 452 2003.
ISSN: ISSN 0949-8257
PubMed: 12761666
Page generated: Sun Oct 13 04:57:05 2024

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