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Chlorine in PDB 5ia1: Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054

Enzymatic activity of Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054

All present enzymatic activity of Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054:
2.7.10.1;

Protein crystallography data

The structure of Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054, PDB code: 5ia1 was solved by D.Kudlinzki, V.L.Linhard, S.L.Gande, S.Sreeramulu, K.Saxena, S.Heinzlmeir, G.Medard, B.Kuester, H.Schwalbe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.26 / 2.04
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 32.714, 106.741, 40.729, 90.00, 108.79, 90.00
R / Rfree (%) 18.1 / 22.3

Other elements in 5ia1:

The structure of Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054 also contains other interesting chemical elements:

Fluorine (F) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054 (pdb code 5ia1). 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 Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054, PDB code: 5ia1:

Chlorine binding site 1 out of 1 in 5ia1

Go back to Chlorine Binding Sites List in 5ia1
Chlorine binding site 1 out of 1 in the Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Ephrin A2 (EPHA2) Receptor Protein Kinase with MLN8054 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1001

b:54.8
occ:1.00
 CL1 A:ZZL1001 0.0 54.8 1.0
C26 A:ZZL1001 1.8 43.1 1.0
C28 A:ZZL1001 2.7 42.0 1.0
C25 A:ZZL1001 2.7 38.0 1.0
CA A:GLY620 3.6 47.1 1.0
N A:GLY622 3.7 57.5 1.0
N A:ALA621 3.8 57.1 1.0
C A:GLY620 4.0 51.8 1.0
CA A:GLY622 4.0 60.7 1.0
C29 A:ZZL1001 4.0 40.6 1.0
C24 A:ZZL1001 4.0 39.5 1.0
CG2 A:VAL627 4.1 41.9 1.0
CB A:VAL627 4.3 41.4 1.0
C30 A:ZZL1001 4.5 40.8 1.0
C A:ALA621 4.6 59.5 1.0
N A:GLY620 4.7 43.5 1.0
O A:ILE619 4.8 41.9 1.0
CA A:ALA621 4.8 59.4 1.0
CG1 A:VAL627 4.8 39.5 1.0
O A:GLY620 4.9 51.4 1.0

Reference:

S.Heinzlmeir, D.Kudlinzki, S.Sreeramulu, S.Klaeger, S.L.Gande, V.Linhard, M.Wilhelm, H.Qiao, D.Helm, B.Ruprecht, K.Saxena, G.Medard, H.Schwalbe, B.Kuster. Chemical Proteomics and Structural Biology Define EPHA2 Inhibition By Clinical Kinase Drugs. Acs Chem. Biol. V. 11 3400 2016.
ISSN: ESSN 1554-8937
PubMed: 27768280
DOI: 10.1021/ACSCHEMBIO.6B00709
Page generated: Sat Jul 12 03:03:01 2025

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