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Chlorine in PDB 3cd3: Crystal Structure of Phosphorylated Human Feline Sarcoma Viral Oncogene Homologue (V-Fes) in Complex with Staurosporine and A Consensus Peptide

Enzymatic activity of Crystal Structure of Phosphorylated Human Feline Sarcoma Viral Oncogene Homologue (V-Fes) in Complex with Staurosporine and A Consensus Peptide

All present enzymatic activity of Crystal Structure of Phosphorylated Human Feline Sarcoma Viral Oncogene Homologue (V-Fes) in Complex with Staurosporine and A Consensus Peptide:
2.7.10.2;

Protein crystallography data

The structure of Crystal Structure of Phosphorylated Human Feline Sarcoma Viral Oncogene Homologue (V-Fes) in Complex with Staurosporine and A Consensus Peptide, PDB code: 3cd3 was solved by P.Filippakopoulos, E.Salah, C.Cooper, S.S.Picaud, J.M.Elkins, F.Von Delft, C.H.Arrowsmith, A.M.Edwards, J.Weigelt, C.Bountra, S.Knapp, Structuralgenomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.35 / 1.98
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 35.451, 76.905, 150.632, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 24.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Phosphorylated Human Feline Sarcoma Viral Oncogene Homologue (V-Fes) in Complex with Staurosporine and A Consensus Peptide (pdb code 3cd3). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Phosphorylated Human Feline Sarcoma Viral Oncogene Homologue (V-Fes) in Complex with Staurosporine and A Consensus Peptide, PDB code: 3cd3:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 3cd3

Go back to Chlorine Binding Sites List in 3cd3
Chlorine binding site 1 out of 2 in the Crystal Structure of Phosphorylated Human Feline Sarcoma Viral Oncogene Homologue (V-Fes) in Complex with Staurosporine and A Consensus Peptide


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 Phosphorylated Human Feline Sarcoma Viral Oncogene Homologue (V-Fes) in Complex with Staurosporine and A Consensus Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl904

b:39.5
occ:1.00
 NH2 A:ARG770 3.4 92.5 1.0
N A:GLN767 3.5 49.7 1.0
CB A:ASN766 3.7 47.6 1.0
CD A:ARG770 3.7 56.5 1.0
CG B:GLU3 3.7 55.4 1.0
CA A:GLN767 3.8 47.6 1.0
C A:ASN766 3.9 45.8 1.0
CB A:GLN767 4.0 45.2 1.0
CD B:GLU3 4.2 44.4 1.0
OE2 B:GLU3 4.2 51.7 1.0
O A:ASN766 4.3 44.8 1.0
CZ A:ARG770 4.3 80.5 1.0
CA A:ASN766 4.4 48.3 1.0
CD2 B:LEU5 4.5 39.1 1.0
NE A:ARG770 4.5 46.1 1.0
CG2 A:VAL724 4.5 49.6 1.0
CB B:GLU3 4.6 45.1 1.0
CG A:GLN767 4.8 52.4 1.0
CD1 B:LEU5 4.9 57.6 1.0
CG A:ASN766 4.9 51.2 1.0
CG A:ARG770 5.0 52.6 1.0

Chlorine binding site 2 out of 2 in 3cd3

Go back to Chlorine Binding Sites List in 3cd3
Chlorine binding site 2 out of 2 in the Crystal Structure of Phosphorylated Human Feline Sarcoma Viral Oncogene Homologue (V-Fes) in Complex with Staurosporine and A Consensus Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Phosphorylated Human Feline Sarcoma Viral Oncogene Homologue (V-Fes) in Complex with Staurosporine and A Consensus Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl905

b:47.8
occ:1.00
 O A:HOH41 2.7 63.6 1.0
C27 A:STU903 3.6 45.0 1.0
CA A:ALA582 3.9 49.3 1.0
N A:ALA582 4.0 51.1 1.0
CB A:ALA582 4.0 50.6 1.0
CD A:ARG581 4.0 53.6 1.0
CG A:ARG581 4.0 47.4 1.0
CB A:ARG581 4.1 38.3 1.0
C A:ARG581 4.3 50.6 1.0
O A:HOH17 4.4 36.5 1.0
O A:ARG581 4.6 44.7 1.0
OD1 A:ASP560 4.8 43.3 1.0
O6 A:STU903 4.8 44.3 1.0
CA A:ARG581 4.9 44.0 1.0
NE A:ARG581 4.9 59.5 1.0

Reference:

P.Filippakopoulos, M.Kofler, O.Hantschel, G.D.Gish, F.Grebien, E.Salah, P.Neudecker, L.E.Kay, B.E.Turk, G.Superti-Furga, T.Pawson, S.Knapp. Structural Coupling of SH2-Kinase Domains Links Fes and Abl Substrate Recognition and Kinase Activation Cell(Cambridge,Mass.) V. 134 793 2008.
ISSN: ISSN 0092-8674
PubMed: 18775312
DOI: 10.1016/J.CELL.2008.07.047
Page generated: Fri Jul 11 03:56:56 2025

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