Atomistry » Chlorine » PDB 1kv1-1l61 » 1kze
Atomistry »
  Chlorine »
    PDB 1kv1-1l61 »
      1kze »

Chlorine in PDB 1kze: Complex of Mbp-C and Bivalent Man-Terminated Glycopeptide

Protein crystallography data

The structure of Complex of Mbp-C and Bivalent Man-Terminated Glycopeptide, PDB code: 1kze was solved by K.K.Ng, A.R.Kolatkar, S.Park-Snyder, H.Feinberg, D.A.Clark, K.Drickamer, W.I.Weis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 60.740, 75.220, 57.420, 90.00, 90.00, 90.00
R / Rfree (%) 21.2 / 24.3

Other elements in 1kze:

The structure of Complex of Mbp-C and Bivalent Man-Terminated Glycopeptide also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Complex of Mbp-C and Bivalent Man-Terminated Glycopeptide (pdb code 1kze). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Complex of Mbp-C and Bivalent Man-Terminated Glycopeptide, PDB code: 1kze:

Chlorine binding site 1 out of 1 in 1kze

Go back to Chlorine Binding Sites List in 1kze
Chlorine binding site 1 out of 1 in the Complex of Mbp-C and Bivalent Man-Terminated Glycopeptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Complex of Mbp-C and Bivalent Man-Terminated Glycopeptide within 5.0Å range:
probe atom residue distance (Å) B Occ
1:Cl503

b:24.0
occ:1.00
O 1:HOH1017 2.9 19.3 1.0
N 1:CYS214 3.1 11.1 1.0
N 1:ASN199 3.1 12.2 1.0
O 1:HOH1018 3.3 24.5 1.0
O 1:HOH1019 3.4 31.4 1.0
CA 1:PRO213 3.6 12.2 1.0
CB 1:ASN199 3.6 12.0 1.0
SG 1:CYS214 3.7 14.3 1.0
C 1:PRO213 3.8 11.3 1.0
CG 1:ASN199 3.8 13.1 1.0
ND2 1:ASN199 3.8 15.6 1.0
CA 1:ASN199 3.9 11.6 1.0
O 1:GLY197 3.9 19.3 1.0
CB 1:CYS214 4.0 14.4 1.0
C 1:GLU198 4.0 12.9 1.0
CA 1:GLU198 4.1 14.2 1.0
CA 1:CYS214 4.1 12.2 1.0
O 1:VAL212 4.2 11.8 1.0
C 1:GLY197 4.3 18.9 1.0
N 1:GLU198 4.4 16.2 1.0
CB 1:PRO213 4.4 12.6 1.0
C 1:ASN199 4.5 10.3 1.0
N 1:CYS200 4.5 10.2 1.0
OD1 1:ASN199 4.6 15.6 1.0
N 1:PRO213 4.7 12.4 1.0
OE1 1:GLN167 4.7 26.1 1.0
C 1:VAL212 4.8 11.2 1.0

Reference:

K.K.Ng, A.R.Kolatkar, S.Park-Snyder, H.Feinberg, D.A.Clark, K.Drickamer, W.I.Weis. Orientation of Bound Ligands in Mannose-Binding Proteins. Implications For Multivalent Ligand Recognition. J.Biol.Chem. V. 277 16088 2002.
ISSN: ISSN 0021-9258
PubMed: 11850428
DOI: 10.1074/JBC.M200493200
Page generated: Fri Jul 19 23:32:53 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy