Phosphorus in PDB 1a1a: C-Src (SH2 Domain with C188A Mutation) Complexed with Ace-Formyl Phosphotyr-Glu-(N,N-Dipentyl Amine)

All present enzymatic activity of C-Src (SH2 Domain with C188A Mutation) Complexed with Ace-Formyl Phosphotyr-Glu-(N,N-Dipentyl Amine):
2.7.1.112;

The structure of C-Src (SH2 Domain with C188A Mutation) Complexed with Ace-Formyl Phosphotyr-Glu-(N,N-Dipentyl Amine), PDB code: 1a1a was solved by L.Shewchuk, S.Jordan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.400, 65.400, 74.600, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / n/a

The binding sites of Phosphorus atom in the C-Src (SH2 Domain with C188A Mutation) Complexed with Ace-Formyl Phosphotyr-Glu-(N,N-Dipentyl Amine) (pdb code 1a1a). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 2 binding sites of Phosphorus where determined in the C-Src (SH2 Domain with C188A Mutation) Complexed with Ace-Formyl Phosphotyr-Glu-(N,N-Dipentyl Amine), PDB code: 1a1a:
Jump to Phosphorus binding site number: 1; 2;

Phosphorus binding site 1 out of 2 in the C-Src (SH2 Domain with C188A Mutation) Complexed with Ace-Formyl Phosphotyr-Glu-(N,N-Dipentyl Amine)


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of C-Src (SH2 Domain with C188A Mutation) Complexed with Ace-Formyl Phosphotyr-Glu-(N,N-Dipentyl Amine) within 5.0Å range: probe atom residue distance (Å) B Occ C:P101 b:38.8 occ:1.00 P C:PTH101 0.0 38.8 1.0 O1P C:PTH101 1.4 42.8 1.0 O3P C:PTH101 1.5 40.9 1.0 O2P C:PTH101 1.6 36.9 1.0 OH C:PTH101 1.7 36.9 1.0 HH22 A:ARG178 2.5 0.0 1.0 CZ C:PTH101 2.6 37.3 1.0 HH12 A:ARG178 2.7 0.0 1.0 HE A:ARG158 2.8 0.0 1.0 HH21 A:ARG158 2.9 0.0 1.0 H A:GLU181 3.0 0.0 1.0 HG1 A:THR182 3.1 0.0 1.0 CE2 C:PTH101 3.4 33.5 1.0 CE1 C:PTH101 3.4 38.5 1.0 H A:THR182 3.5 0.0 1.0 NH2 A:ARG178 3.5 20.5 1.0 NH1 A:ARG178 3.6 21.1 1.0 NE A:ARG158 3.7 44.0 1.0 CF C:PTH101 3.8 44.4 1.0 NH2 A:ARG158 3.8 47.8 1.0 N A:GLU181 3.9 29.6 1.0 OG1 A:THR182 3.9 35.5 1.0 CZ A:ARG178 4.0 25.2 1.0 OG A:SER188 4.2 48.2 1.0 HH21 A:ARG178 4.2 0.0 1.0 CZ A:ARG158 4.3 42.7 1.0 CB A:ARG158 4.3 27.4 1.0 HOF C:PTH101 4.3 0.0 1.0 OG A:SER180 4.4 38.5 1.0 N A:THR182 4.4 33.2 1.0 CB A:GLU181 4.4 30.3 1.0 HH11 A:ARG178 4.4 0.0 1.0 HZ2 A:LYS206 4.5 0.0 1.0 CD1 C:PTH101 4.6 36.3 1.0 CG A:ARG158 4.6 36.0 1.0 CD2 C:PTH101 4.6 32.7 1.0 HH22 A:ARG158 4.6 0.0 1.0 HG A:SER188 4.6 0.0 1.0 OF C:PTH101 4.6 59.7 1.0 CA A:SER180 4.6 31.9 1.0 CA A:GLU181 4.7 31.0 1.0 C A:SER180 4.7 28.6 1.0 CG A:GLU181 4.7 32.8 1.0 CD A:ARG158 4.7 35.0 1.0 CG2 A:THR182 4.8 29.9 1.0 CB A:SER188 4.9 36.4 1.0 CB A:THR182 4.9 33.3 1.0 H A:ARG158 5.0 0.0 1.0 CB A:SER180 5.0 30.9 1.0

Phosphorus binding site 2 out of 2 in the C-Src (SH2 Domain with C188A Mutation) Complexed with Ace-Formyl Phosphotyr-Glu-(N,N-Dipentyl Amine)


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of C-Src (SH2 Domain with C188A Mutation) Complexed with Ace-Formyl Phosphotyr-Glu-(N,N-Dipentyl Amine) within 5.0Å range: probe atom residue distance (Å) B Occ D:P101 b:41.4 occ:1.00 P D:PTH101 0.0 41.4 1.0 O1P D:PTH101 1.4 41.3 1.0 O3P D:PTH101 1.5 43.4 1.0 O2P D:PTH101 1.5 41.0 1.0 OH D:PTH101 1.7 43.2 1.0 HH22 B:ARG178 2.7 0.0 1.0 HF2 D:PTH101 2.7 0.0 1.0 CZ D:PTH101 2.7 48.0 1.0 HH12 B:ARG178 2.9 0.0 1.0 HE B:ARG158 2.9 0.0 1.0 HH21 B:ARG158 3.0 0.0 1.0 CF D:PTH101 3.4 47.9 1.0 H B:GLU181 3.4 0.0 1.0 CE1 D:PTH101 3.5 46.7 1.0 CE2 D:PTH101 3.6 47.8 1.0 HG1 B:THR182 3.6 0.0 1.0 NH2 B:ARG178 3.6 25.1 1.0 H B:THR182 3.7 0.0 1.0 NH1 B:ARG178 3.8 27.2 1.0 NE B:ARG158 3.8 38.0 1.0 H1 B:HOH589 3.8 0.0 1.0 NH2 B:ARG158 3.9 36.2 1.0 H1 B:HOH683 3.9 0.0 1.0 O B:HOH683 4.1 89.2 1.0 CZ B:ARG178 4.2 26.3 1.0 CG2 B:THR182 4.2 66.5 1.0 HG B:SER188 4.3 0.0 1.0 OG B:SER188 4.3 33.2 1.0 N B:GLU181 4.3 57.4 1.0 H1 B:HOH688 4.3 0.0 1.0 OG1 B:THR182 4.4 66.2 1.0 CB B:GLU181 4.4 61.7 1.0 HH21 B:ARG178 4.4 0.0 1.0 CB B:ARG158 4.4 28.8 1.0 CZ B:ARG158 4.4 33.1 1.0 CG B:GLU181 4.5 65.8 1.0 OF D:PTH101 4.6 55.1 1.0 N B:THR182 4.6 63.2 1.0 HH11 B:ARG178 4.6 0.0 1.0 O B:HOH688 4.6 80.2 1.0 HH22 B:ARG158 4.7 0.0 1.0 CD1 D:PTH101 4.7 42.4 1.0 OE1 B:GLU181 4.7 77.3 1.0 O B:HOH589 4.8 53.4 1.0 CD B:GLU181 4.8 70.1 1.0 CD2 D:PTH101 4.8 45.6 1.0 H2 B:HOH530 4.8 0.0 1.0 CB B:THR182 4.9 63.6 1.0 CD B:ARG158 4.9 36.6 1.0 CA B:GLU181 4.9 60.7 1.0 OG B:SER180 4.9 61.7 1.0 CG B:ARG158 4.9 33.1 1.0

P.S.Charifson, L.M.Shewchuk, W.Rocque, C.W.Hummel, S.R.Jordan, C.Mohr, G.J.Pacofsky, M.R.Peel, M.Rodriguez, D.D.Sternbach, T.G.Consler. Peptide Ligands of PP60(C-Src) SH2 Domains: A Thermodynamic and Structural Study. Biochemistry V. 36 6283 1997.
ISSN: ISSN 0006-2960
PubMed: 9174343
DOI: 10.1021/BI970019N