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Zinc in PDB 1x1d: Crystal Structure of Bchu Complexed with S-Adenosyl-L-Homocysteine and Zn-Bacteriopheophorbide D

Protein crystallography data

The structure of Crystal Structure of Bchu Complexed with S-Adenosyl-L-Homocysteine and Zn-Bacteriopheophorbide D, PDB code: 1x1d was solved by H.Yamaguchi, K.Wada, K.Fukuyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.99 / 2.70
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 81.613, 81.613, 251.650, 90.00, 90.00, 120.00
R / Rfree (%) 23.7 / 28.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Bchu Complexed with S-Adenosyl-L-Homocysteine and Zn-Bacteriopheophorbide D (pdb code 1x1d). 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 Bchu Complexed with S-Adenosyl-L-Homocysteine and Zn-Bacteriopheophorbide D, PDB code: 1x1d:

Zinc binding site 1 out of 1 in 1x1d

Go back to Zinc Binding Sites List in 1x1d
Zinc binding site 1 out of 1 in the Crystal Structure of Bchu Complexed with S-Adenosyl-L-Homocysteine and Zn-Bacteriopheophorbide D


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 Bchu Complexed with S-Adenosyl-L-Homocysteine and Zn-Bacteriopheophorbide D within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn5001

b:30.1
occ:0.10
CE1 A:HIS290 2.8 87.0 1.0
NE2 A:HIS290 3.4 82.8 1.0
NE2 A:HIS150 3.5 68.1 1.0
ND1 A:HIS290 3.5 74.7 1.0
CD2 A:HIS150 4.3 65.4 1.0
CD2 A:HIS290 4.4 78.6 1.0
CE1 A:HIS150 4.4 71.2 1.0
CG A:HIS290 4.5 69.8 1.0

Reference:

K.Wada, H.Yamaguchi, J.Harada, K.Niimi, S.Osumi, Y.Saga, H.Oh-Oka, H.Tamiaki, K.Fukuyama. Crystal Structures of Bchu, A Methyltransferase Involved in Bacteriochlorophyll C Biosynthesis, and Its Complex with S-Adenosylhomocysteine: Implications For Reaction Mechanism. J.Mol.Biol. V. 360 839 2006.
ISSN: ISSN 0022-2836
PubMed: 16797589
DOI: 10.1016/J.JMB.2006.05.057
Page generated: Wed Dec 16 03:10:54 2020

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