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Vanadium in PDB 2hy3: Crystal Structure of the Human Tyrosine Receptor Phosphate Gamma in Complex with Vanadate

Enzymatic activity of Crystal Structure of the Human Tyrosine Receptor Phosphate Gamma in Complex with Vanadate

All present enzymatic activity of Crystal Structure of the Human Tyrosine Receptor Phosphate Gamma in Complex with Vanadate:
3.1.3.48;

Protein crystallography data

The structure of Crystal Structure of the Human Tyrosine Receptor Phosphate Gamma in Complex with Vanadate, PDB code: 2hy3 was solved by X.Jin, T.Min, A.Bera, H.Mu, J.M.Sauder, J.C.Freeman, C.Reyes, D.Smith, S.R.Wasserman, S.K.Burley, L.Shapiro, New York Sgx Research Center Forstructural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.00 / 2.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 58.173, 74.787, 82.071, 90.00, 99.58, 90.00
R / Rfree (%) 20.2 / 28.8

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Crystal Structure of the Human Tyrosine Receptor Phosphate Gamma in Complex with Vanadate (pdb code 2hy3). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total 2 binding sites of Vanadium where determined in the Crystal Structure of the Human Tyrosine Receptor Phosphate Gamma in Complex with Vanadate, PDB code: 2hy3:
Jump to Vanadium binding site number: 1; 2;

Vanadium binding site 1 out of 2 in 2hy3

Go back to Vanadium Binding Sites List in 2hy3
Vanadium binding site 1 out of 2 in the Crystal Structure of the Human Tyrosine Receptor Phosphate Gamma in Complex with Vanadate


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Crystal Structure of the Human Tyrosine Receptor Phosphate Gamma in Complex with Vanadate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V158

b:70.4
occ:1.00
V A:VO4158 0.0 70.4 1.0
O4 A:VO4158 1.9 62.3 1.0
O2 A:VO4158 1.9 64.3 1.0
O3 A:VO4158 1.9 63.5 1.0
O1 A:VO4158 1.9 63.6 1.0
SG A:CYS1060 3.0 42.1 1.0
N A:GLY1065 3.7 35.6 1.0
N A:ALA1062 3.7 34.5 1.0
OE1 A:GLN1104 3.9 44.2 1.0
N A:SER1061 4.0 38.5 1.0
CA A:GLY1065 4.1 36.1 1.0
CB A:ALA1062 4.1 34.8 1.0
CB A:CYS1060 4.2 39.8 1.0
N A:GLY1063 4.2 35.5 1.0
N A:ARG1066 4.3 38.2 1.0
CA A:ALA1062 4.3 35.2 1.0
N A:VAL1064 4.4 35.7 1.0
CB A:SER1061 4.4 37.6 1.0
CA A:SER1061 4.5 37.7 1.0
C A:SER1061 4.5 36.6 1.0
C A:ALA1062 4.6 35.1 1.0
C A:GLY1065 4.7 36.4 1.0
C A:VAL1064 4.8 35.4 1.0
CG A:ARG1066 4.9 40.9 1.0
CG2 A:VAL1064 4.9 31.4 1.0
C A:CYS1060 5.0 39.0 1.0
CD A:GLN1104 5.0 42.8 1.0

Vanadium binding site 2 out of 2 in 2hy3

Go back to Vanadium Binding Sites List in 2hy3
Vanadium binding site 2 out of 2 in the Crystal Structure of the Human Tyrosine Receptor Phosphate Gamma in Complex with Vanadate


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 2 of Crystal Structure of the Human Tyrosine Receptor Phosphate Gamma in Complex with Vanadate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:V159

b:61.0
occ:1.00
V B:VO4159 0.0 61.0 1.0
O1 B:VO4159 1.9 56.1 1.0
O2 B:VO4159 1.9 59.3 1.0
O4 B:VO4159 1.9 55.7 1.0
O3 B:VO4159 1.9 58.5 1.0
SG B:CYS1060 2.9 38.1 1.0
N B:GLY1065 3.6 38.3 1.0
N B:ALA1062 3.8 37.0 1.0
N B:GLY1063 3.9 35.6 1.0
CB B:ALA1062 3.9 35.2 1.0
N B:ARG1066 4.0 39.0 1.0
CA B:GLY1065 4.1 38.6 1.0
N B:VAL1064 4.1 38.0 1.0
CB B:CYS1060 4.1 39.5 1.0
N B:SER1061 4.2 39.1 1.0
CA B:ALA1062 4.2 36.2 1.0
CG2 B:VAL1064 4.5 33.7 1.0
C B:ALA1062 4.5 36.0 1.0
C B:GLY1065 4.6 39.4 1.0
C B:VAL1064 4.6 38.2 1.0
C B:SER1061 4.7 38.2 1.0
CA B:SER1061 4.8 39.0 1.0
CA B:GLY1063 4.8 36.3 1.0
CB B:SER1061 4.8 39.1 1.0
CA B:VAL1064 4.8 37.2 1.0
C B:GLY1063 5.0 37.6 1.0

Reference:

S.C.Almo, J.B.Bonanno, J.M.Sauder, S.Emtage, T.P.Dilorenzo, V.Malashkevich, S.R.Wasserman, S.Swaminathan, S.Eswaramoorthy, R.Agarwal, D.Kumaran, M.Madegowda, S.Ragumani, Y.Patskovsky, J.Alvarado, U.A.Ramagopal, J.Faber-Barata, M.R.Chance, A.Sali, A.Fiser, Z.Y.Zhang, D.S.Lawrence, S.K.Burley. Structural Genomics of Protein Phosphatases. J.Struct.Funct.Genom. V. 8 121 2007.
ISSN: ISSN 1345-711X
PubMed: 18058037
DOI: 10.1007/S10969-007-9036-1
Page generated: Wed Dec 16 02:30:38 2020

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