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Vanadium in PDB 4qih: The Structure of Mycobacterial Glucosyl-3-Phosphoglycerate Phosphatase RV2419C Complexes with VO3

Enzymatic activity of The Structure of Mycobacterial Glucosyl-3-Phosphoglycerate Phosphatase RV2419C Complexes with VO3

All present enzymatic activity of The Structure of Mycobacterial Glucosyl-3-Phosphoglycerate Phosphatase RV2419C Complexes with VO3:
3.1.3.70;

Protein crystallography data

The structure of The Structure of Mycobacterial Glucosyl-3-Phosphoglycerate Phosphatase RV2419C Complexes with VO3, PDB code: 4qih was solved by W.H.Zhou, Q.Q.Zheng, D.Q.Jiang, W.Zhang, Q.Q.Zhang, J.Jin, X.Li, H.T.Yang, N.Shaw, Z.Rao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.01 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.312, 82.762, 131.319, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 24.5

Vanadium Binding Sites:

The binding sites of Vanadium atom in the The Structure of Mycobacterial Glucosyl-3-Phosphoglycerate Phosphatase RV2419C Complexes with VO3 (pdb code 4qih). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total 2 binding sites of Vanadium where determined in the The Structure of Mycobacterial Glucosyl-3-Phosphoglycerate Phosphatase RV2419C Complexes with VO3, PDB code: 4qih:
Jump to Vanadium binding site number: 1; 2;

Vanadium binding site 1 out of 2 in 4qih

Go back to Vanadium Binding Sites List in 4qih
Vanadium binding site 1 out of 2 in the The Structure of Mycobacterial Glucosyl-3-Phosphoglycerate Phosphatase RV2419C Complexes with VO3


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of The Structure of Mycobacterial Glucosyl-3-Phosphoglycerate Phosphatase RV2419C Complexes with VO3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V601

b:33.3
occ:1.00
V A:VN3601 0.0 33.3 1.0
O2 A:VN3601 1.6 32.1 1.0
O1 A:VN3601 1.6 28.3 1.0
O3 A:VN3601 1.6 30.1 1.0
NE2 A:HIS11 2.1 28.9 1.0
O A:HOH766 2.3 26.8 1.0
HE A:ARG10 2.9 35.8 1.0
HH21 A:ARG10 3.0 36.8 1.0
CE1 A:HIS11 3.1 28.8 1.0
CD2 A:HIS11 3.1 31.9 1.0
HE22 A:GLN23 3.2 43.4 1.0
HE1 A:HIS11 3.2 34.5 1.0
HB3 A:HIS159 3.2 34.8 1.0
HH11 A:ARG60 3.2 44.0 1.0
HD2 A:HIS11 3.3 38.3 1.0
HD1 A:HIS159 3.4 35.6 1.0
H A:GLY160 3.6 40.0 1.0
HE21 A:GLN23 3.7 43.4 1.0
NE2 A:GLN23 3.7 36.1 1.0
NE A:ARG10 3.8 29.8 1.0
NH2 A:ARG10 3.8 30.7 1.0
HD21 A:ASN17 3.8 42.3 1.0
HD2 A:ARG60 3.9 40.6 1.0
HA A:HIS159 3.9 40.2 1.0
OE2 A:GLU84 3.9 24.8 1.0
NH1 A:ARG60 4.0 36.7 1.0
CB A:HIS159 4.1 29.0 1.0
HG2 A:GLU84 4.1 37.2 1.0
ND1 A:HIS159 4.2 29.6 1.0
ND1 A:HIS11 4.2 33.1 1.0
HH12 A:ARG60 4.2 44.0 1.0
CG A:HIS11 4.2 33.7 1.0
CZ A:ARG10 4.3 28.3 1.0
O A:HOH701 4.3 14.2 1.0
N A:GLY160 4.4 33.3 1.0
HG3 A:ARG10 4.4 35.0 1.0
CA A:HIS159 4.5 33.5 1.0
HH22 A:ARG10 4.5 36.8 1.0
HB2 A:GLU84 4.6 34.1 1.0
CG A:HIS159 4.6 31.1 1.0
ND2 A:ASN17 4.7 35.3 1.0
CD A:GLU84 4.7 30.3 1.0
CD A:ARG60 4.7 33.9 1.0
CG A:GLU84 4.8 31.0 1.0
HB2 A:HIS159 4.8 34.8 1.0
CD A:ARG10 4.8 30.8 1.0
HD3 A:ARG60 4.9 40.6 1.0
HD1 A:HIS11 5.0 39.7 1.0
HD2 A:ARG10 5.0 37.0 1.0
CD A:GLN23 5.0 31.7 1.0
C A:HIS159 5.0 28.7 1.0

Vanadium binding site 2 out of 2 in 4qih

Go back to Vanadium Binding Sites List in 4qih
Vanadium binding site 2 out of 2 in the The Structure of Mycobacterial Glucosyl-3-Phosphoglycerate Phosphatase RV2419C Complexes with VO3


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 2 of The Structure of Mycobacterial Glucosyl-3-Phosphoglycerate Phosphatase RV2419C Complexes with VO3 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:V601

b:42.7
occ:1.00
V B:VN3601 0.0 42.7 1.0
O1 B:VN3601 1.6 41.3 1.0
O2 B:VN3601 1.6 45.9 1.0
O3 B:VN3601 1.6 46.3 1.0
NE2 B:HIS11 2.1 41.2 1.0
O B:HOH720 2.3 29.9 1.0
HH11 B:ARG10 2.8 54.0 1.0
HE22 B:GLN23 2.8 55.1 1.0
CD2 B:HIS11 3.0 40.5 1.0
HE B:ARG60 3.1 52.9 1.0
HD2 B:HIS11 3.1 48.6 1.0
CE1 B:HIS11 3.1 43.7 1.0
HB3 B:HIS159 3.3 48.6 1.0
HE1 B:HIS11 3.3 52.5 1.0
NE2 B:GLN23 3.4 45.9 1.0
HE21 B:GLN23 3.4 55.1 1.0
H B:GLY160 3.6 47.4 1.0
NH1 B:ARG10 3.6 45.0 1.0
HD2 B:ARG10 3.6 55.9 1.0
HH21 B:ARG60 3.7 48.9 1.0
HH12 B:ARG10 3.7 54.0 1.0
HD21 B:ASN17 3.7 44.6 1.0
OE2 B:GLU84 3.8 37.1 1.0
NE B:ARG60 3.9 44.1 1.0
ND1 B:HIS159 4.0 50.8 1.0
HA B:HIS159 4.1 49.8 1.0
CG B:HIS11 4.1 41.9 1.0
ND1 B:HIS11 4.2 46.7 1.0
CB B:HIS159 4.2 40.5 1.0
HG2 B:GLU84 4.2 54.3 1.0
O B:HOH719 4.3 30.6 1.0
N B:GLY160 4.4 39.5 1.0
NH2 B:ARG60 4.4 40.7 1.0
HD2 B:ARG60 4.4 57.2 1.0
HG3 B:ARG10 4.5 55.1 1.0
CD B:ARG10 4.5 46.6 1.0
ND2 B:ASN17 4.6 37.2 1.0
CG B:HIS159 4.6 51.4 1.0
CA B:HIS159 4.6 41.5 1.0
CZ B:ARG60 4.7 54.2 1.0
CD B:GLU84 4.7 45.7 1.0
CD B:GLN23 4.7 48.1 1.0
HB2 B:GLU84 4.7 50.0 1.0
CZ B:ARG10 4.7 42.2 1.0
CD B:ARG60 4.8 47.6 1.0
CG B:GLU84 4.9 45.2 1.0
HB2 B:HIS159 4.9 48.6 1.0
HD1 B:HIS11 5.0 56.0 1.0
HB2 B:GLN23 5.0 59.2 1.0
CG B:ARG10 5.0 45.9 1.0

Reference:

Q.Zheng, D.Jiang, W.Zhang, Q.Zhang, Q.Zhao, J.Jin, X.Li, H.Yang, M.Bartlam, N.Shaw, W.Zhou, Z.Rao. Mechanism of Dephosphorylation of Glucosyl-3-Phosphoglycerate By A Histidine Phosphatase J.Biol.Chem. V. 289 21242 2014.
ISSN: ISSN 0021-9258
PubMed: 24914210
DOI: 10.1074/JBC.M114.569913
Page generated: Wed Dec 16 02:31:13 2020

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