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Zinc in PDB 3igd: Crystal Structure of Mtu Reca Intein, Splicing Domain

Protein crystallography data

The structure of Crystal Structure of Mtu Reca Intein, Splicing Domain, PDB code: 3igd was solved by P.Van Roey, M.Belfort, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.69 / 2.40
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 90.150, 90.150, 39.460, 90.00, 90.00, 90.00
R / Rfree (%) 28.9 / 33.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Mtu Reca Intein, Splicing Domain (pdb code 3igd). 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 Mtu Reca Intein, Splicing Domain, PDB code: 3igd:

Zinc binding site 1 out of 1 in 3igd

Go back to Zinc Binding Sites List in 3igd
Zinc binding site 1 out of 1 in the Crystal Structure of Mtu Reca Intein, Splicing Domain


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 Mtu Reca Intein, Splicing Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:62.5
occ:1.00
ND1 A:HIS429 1.7 62.6 1.0
OE1 A:GLU424 2.0 43.5 1.0
CE1 A:HIS429 2.3 61.1 1.0
N1 A:SNN440 2.7 66.2 1.0
CD A:GLU424 2.8 47.2 1.0
CG A:GLU424 2.8 46.4 1.0
O5 A:SNN440 2.9 61.1 1.0
CG A:HIS429 3.0 62.8 1.0
C5 A:SNN440 3.2 65.7 1.0
NE2 A:HIS429 3.6 62.4 1.0
CB A:HIS429 3.7 61.1 1.0
CD2 A:HIS429 3.9 60.8 1.0
C2 A:SNN440 3.9 66.5 1.0
OE2 A:GLU424 4.0 47.9 1.0
CA A:HIS429 4.2 60.3 1.0
CB A:GLU424 4.2 51.2 1.0
O A:HIS429 4.4 59.3 1.0
O2 A:SNN440 4.4 67.3 1.0
CA A:GLU424 4.6 51.5 1.0
C4 A:SNN440 4.6 65.9 1.0
C A:HIS429 4.7 59.0 1.0
N A:VAL425 4.7 55.5 1.0
C3 A:SNN440 5.0 64.7 1.0

Reference:

K.Hiraga, I.Soga, J.T.Dansereau, B.Pereira, V.Derbyshire, Z.Du, C.Wang, P.Van Roey, G.Belfort, M.Belfort. Selection and Structure of Hyperactive Inteins: Peripheral Changes Relayed to the Catalytic Center. J.Mol.Biol. V. 393 1106 2009.
ISSN: ISSN 0022-2836
PubMed: 19744499
DOI: 10.1016/J.JMB.2009.08.074
Page generated: Wed Dec 16 04:26:18 2020

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