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Chlorine in PDB 4mv4: Crystal Structure of Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2

Enzymatic activity of Crystal Structure of Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2

All present enzymatic activity of Crystal Structure of Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2:
6.3.4.14; 6.4.1.2;

Protein crystallography data

The structure of Crystal Structure of Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2, PDB code: 4mv4 was solved by T.C.Broussard, S.Pakhomova, D.B.Neau, T.S.Champion, R.J.Bonnot, G.L.Waldrop, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.60 / 1.61
Space group P 64
Cell size a, b, c (Å), α, β, γ (°) 85.344, 85.344, 104.217, 90.00, 90.00, 120.00
R / Rfree (%) 15.4 / 18.4

Other elements in 4mv4:

The structure of Crystal Structure of Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2 also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2 (pdb code 4mv4). 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 Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2, PDB code: 4mv4:

Chlorine binding site 1 out of 1 in 4mv4

Go back to Chlorine Binding Sites List in 4mv4
Chlorine binding site 1 out of 1 in the Crystal Structure of Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2


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 Biotin Carboxylase From Haemophilus Influenzae in Complex with Amppcp and MG2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl504

b:27.0
occ:1.00
HH12 A:ARG292 1.9 30.8 1.0
H A:VAL295 2.4 18.2 1.0
NH1 A:ARG292 2.5 25.7 1.0
HA A:GLN294 2.8 23.2 1.0
O A:HOH745 2.9 37.9 1.0
HH11 A:ARG292 3.0 30.8 1.0
O A:HOH895 3.0 29.5 1.0
HG22 A:VAL295 3.0 23.8 1.0
HH22 A:ARG292 3.1 31.6 1.0
HG2 A:GLN294 3.2 22.8 1.0
HB2 A:TYR82 3.2 18.9 1.0
N A:VAL295 3.2 15.2 1.0
HB3 A:GLN294 3.3 25.4 1.0
CZ A:ARG292 3.4 23.6 1.0
HG21 A:VAL295 3.4 23.8 1.0
NH2 A:ARG292 3.5 26.3 1.0
CA A:GLN294 3.6 19.3 1.0
CG2 A:VAL295 3.6 19.8 1.0
HE22 A:GLN294 3.7 56.9 1.0
CB A:GLN294 3.7 21.2 1.0
HB A:VAL295 3.8 17.2 1.0
CG A:GLN294 3.9 19.0 1.0
CB A:TYR82 3.9 15.8 1.0
C A:GLN294 3.9 14.8 1.0
HB3 A:TYR82 4.0 18.9 1.0
CG A:TYR82 4.1 13.8 1.0
CB A:VAL295 4.1 14.4 1.0
O A:HOH665 4.2 34.7 1.0
CA A:VAL295 4.2 12.5 1.0
HH21 A:ARG292 4.3 31.6 1.0
NE2 A:GLN294 4.3 47.4 1.0
OE2 A:GLU296 4.4 16.1 1.0
HG23 A:VAL295 4.4 23.8 1.0
O A:ILE293 4.5 18.5 1.0
NE A:ARG292 4.5 34.7 1.0
CD1 A:TYR82 4.5 15.7 1.0
CD2 A:TYR82 4.5 14.9 1.0
HD2 A:ARG292 4.5 32.4 1.0
O A:HOH848 4.5 41.0 1.0
HH22 A:ARG338 4.6 28.0 1.0
CD A:GLN294 4.6 30.9 1.0
HD2 A:TYR82 4.6 17.9 1.0
HD1 A:TYR82 4.6 18.9 1.0
HG3 A:GLN294 4.7 22.8 1.0
HB2 A:GLN294 4.7 25.4 1.0
HA A:VAL295 4.7 15.0 1.0
N A:GLN294 4.8 20.0 1.0
H A:GLU296 4.9 17.9 1.0
HE21 A:GLN294 5.0 56.9 1.0

Reference:

T.C.Broussard, S.Pakhomova, D.B.Neau, T.S.Champion, R.J.Bonnot, G.L.Waldrop. Structure of Biotin Carboxylase To Be Published.
Page generated: Sun Jul 21 20:12:16 2024

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