Atomistry » Iodine » PDB 1q0t-1v1f » 1rtk
Atomistry »
  Iodine »
    PDB 1q0t-1v1f »
      1rtk »

Iodine in PDB 1rtk: Crystal Structure Analysis of the Bb Segment of Factor B Complexed with 4-Guanidinobenzoic Acid

Enzymatic activity of Crystal Structure Analysis of the Bb Segment of Factor B Complexed with 4-Guanidinobenzoic Acid

All present enzymatic activity of Crystal Structure Analysis of the Bb Segment of Factor B Complexed with 4-Guanidinobenzoic Acid:
3.4.21.47;

Protein crystallography data

The structure of Crystal Structure Analysis of the Bb Segment of Factor B Complexed with 4-Guanidinobenzoic Acid, PDB code: 1rtk was solved by K.Ponnuraj, Y.Xu, K.Macon, D.Moore, J.E.Volanakis, S.V.Narayana, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.81 / 2.30
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 98.355, 98.355, 125.657, 90.00, 90.00, 120.00
R / Rfree (%) 20.8 / 24.5

Other elements in 1rtk:

The structure of Crystal Structure Analysis of the Bb Segment of Factor B Complexed with 4-Guanidinobenzoic Acid also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Sodium (Na) 7 atoms

Iodine Binding Sites:

The binding sites of Iodine atom in the Crystal Structure Analysis of the Bb Segment of Factor B Complexed with 4-Guanidinobenzoic Acid (pdb code 1rtk). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total 2 binding sites of Iodine where determined in the Crystal Structure Analysis of the Bb Segment of Factor B Complexed with 4-Guanidinobenzoic Acid, PDB code: 1rtk:
Jump to Iodine binding site number: 1; 2;

Iodine binding site 1 out of 2 in 1rtk

Go back to Iodine Binding Sites List in 1rtk
Iodine binding site 1 out of 2 in the Crystal Structure Analysis of the Bb Segment of Factor B Complexed with 4-Guanidinobenzoic Acid


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of Crystal Structure Analysis of the Bb Segment of Factor B Complexed with 4-Guanidinobenzoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:I740

b:31.9
occ:1.00
CE1 A:HIS531 3.5 27.4 1.0
NE2 A:HIS531 3.8 30.2 1.0
CD A:PRO725 3.9 23.9 1.0
N A:TRP726 4.0 23.0 1.0
CA A:VAL723 4.0 23.6 1.0
CB A:PRO725 4.0 24.8 1.0
CB A:TRP726 4.2 22.3 1.0
CG A:PRO725 4.2 23.0 1.0
C A:VAL723 4.2 24.4 1.0
O A:GLN722 4.2 25.8 1.0
O A:VAL723 4.2 23.3 1.0
CE2 A:TYR550 4.4 24.2 1.0
N A:PRO725 4.4 26.1 1.0
CA A:PRO725 4.6 24.7 1.0
CA A:TRP726 4.7 23.1 1.0
ND1 A:HIS531 4.7 27.8 1.0
C A:PRO725 4.7 25.5 1.0
CB A:VAL723 4.7 24.1 1.0
CD2 A:TYR550 4.9 22.8 1.0
N A:LEU724 4.9 25.7 1.0
N A:VAL723 5.0 23.1 1.0

Iodine binding site 2 out of 2 in 1rtk

Go back to Iodine Binding Sites List in 1rtk
Iodine binding site 2 out of 2 in the Crystal Structure Analysis of the Bb Segment of Factor B Complexed with 4-Guanidinobenzoic Acid


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 2 of Crystal Structure Analysis of the Bb Segment of Factor B Complexed with 4-Guanidinobenzoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:I741

b:29.2
occ:1.00
O A:HOH1010 3.1 25.9 1.0
NA A:NA748 3.4 32.0 1.0
O A:HOH860 3.5 18.7 1.0
CE1 A:HIS466 3.6 20.3 1.0
CB A:GLN565 4.1 25.5 1.0
NE2 A:GLN565 4.1 33.3 1.0
CG2 A:THR566 4.2 19.6 1.0
NE2 A:HIS466 4.3 22.0 1.0
ND1 A:HIS466 4.6 23.7 1.0
N A:GLN565 4.9 22.3 1.0
CA A:GLN565 4.9 22.6 1.0
CG A:GLN565 5.0 28.1 1.0

Reference:

K.Ponnuraj, Y.Xu, K.Macon, D.Moore, J.E.Volanakis, S.V.Narayana. Structural Analysis of Engineered Bb Fragment of Complement Factor B: Insights Into the Activation Mechanism of the Alternative Pathway C3-Convertase. Mol.Cell V. 14 17 2004.
ISSN: ISSN 1097-2765
PubMed: 15068800
DOI: 10.1016/S1097-2765(04)00160-1
Page generated: Sun Dec 13 19:21:10 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy