Atomistry » Zinc » PDB 6iu6-6j4b » 6ivm
Atomistry »
  Zinc »
    PDB 6iu6-6j4b »
      6ivm »

Zinc in PDB 6ivm: Crystal Structure of A Membrane Protein P143A

Protein crystallography data

The structure of Crystal Structure of A Membrane Protein P143A, PDB code: 6ivm was solved by A.Kittredge, F.Fukuda, Y.Zhang, T.Yang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.72 / 2.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 113.965, 158.808, 161.682, 90.00, 90.00, 90.00
R / Rfree (%) 20.8 / 24.3

Other elements in 6ivm:

The structure of Crystal Structure of A Membrane Protein P143A also contains other interesting chemical elements:

Chlorine (Cl) 12 atoms
Sodium (Na) 1 atom

Zinc Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 17;

Binding sites:

The binding sites of Zinc atom in the Crystal Structure of A Membrane Protein P143A (pdb code 6ivm). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 17 binding sites of Zinc where determined in the Crystal Structure of A Membrane Protein P143A, PDB code: 6ivm:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 17 in 6ivm

Go back to Zinc Binding Sites List in 6ivm
Zinc binding site 1 out of 17 in the Crystal Structure of A Membrane Protein P143A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of A Membrane Protein P143A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:67.3
occ:1.00
OE2 A:GLU191 1.9 71.0 1.0
CL A:CL305 2.0 71.7 1.0
NE2 E:HIS194 2.1 55.3 1.0
O E:HOH408 2.4 57.0 1.0
CD A:GLU191 2.8 68.2 1.0
CD2 E:HIS194 3.0 53.7 1.0
CE1 E:HIS194 3.0 56.2 1.0
OE1 A:GLU191 3.1 70.8 1.0
ND1 E:HIS194 4.1 56.4 1.0
CG E:HIS194 4.1 52.3 1.0
CG A:GLU191 4.2 62.5 1.0
CE A:LYS188 4.3 67.0 1.0
CD A:LYS188 4.5 68.2 1.0
CG2 A:ILE91 4.5 44.0 1.0
CB E:ASP190 4.8 68.3 1.0

Zinc binding site 2 out of 17 in 6ivm

Go back to Zinc Binding Sites List in 6ivm
Zinc binding site 2 out of 17 in the Crystal Structure of A Membrane Protein P143A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of A Membrane Protein P143A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:77.2
occ:1.00
CL B:CL305 1.9 83.0 1.0
NE2 A:HIS194 2.2 46.9 1.0
OE1 B:GLU191 2.3 68.8 1.0
O A:HOH415 2.4 51.2 1.0
OE2 B:GLU191 2.6 72.0 1.0
CD B:GLU191 2.8 70.9 1.0
CD2 A:HIS194 3.2 43.8 1.0
CE1 A:HIS194 3.2 49.4 1.0
CE B:LYS188 4.1 59.3 1.0
CG B:GLU191 4.3 65.5 1.0
ND1 A:HIS194 4.3 48.6 1.0
CG A:HIS194 4.4 44.5 1.0
CG2 B:ILE91 4.6 37.9 1.0
CD B:LYS188 4.7 54.3 1.0
CB A:ASP190 4.9 64.8 1.0
O A:ASP190 5.0 54.8 1.0

Zinc binding site 3 out of 17 in 6ivm

Go back to Zinc Binding Sites List in 6ivm
Zinc binding site 3 out of 17 in the Crystal Structure of A Membrane Protein P143A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of A Membrane Protein P143A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn303

b:73.5
occ:1.00
ND1 A:HIS111 2.1 73.0 1.0
ND1 A:HIS108 2.2 0.6 1.0
CL A:CL307 2.3 96.9 1.0
CL A:CL306 2.5 92.5 1.0
CE1 A:HIS111 3.1 73.3 1.0
CE1 A:HIS108 3.1 0.3 1.0
CG A:HIS108 3.1 93.1 1.0
CG A:HIS111 3.2 74.7 1.0
CB A:HIS108 3.5 87.0 1.0
CB A:HIS111 3.5 73.9 1.0
CA A:HIS108 3.5 85.3 1.0
NE2 A:HIS108 4.2 0.6 1.0
NE2 A:HIS111 4.2 73.1 1.0
CD2 A:HIS108 4.2 92.8 1.0
CD2 A:HIS111 4.3 72.8 1.0
N A:HIS108 4.3 91.1 1.0
O A:HIS108 4.6 84.9 1.0
CG2 A:THR287 4.6 70.6 1.0
C A:HIS108 4.6 82.6 1.0
OE1 A:GLN289 4.8 1.0 1.0
C A:GLU107 4.9 91.2 1.0
N A:GLN289 4.9 0.6 1.0
O A:PRO105 5.0 83.2 1.0
O A:GLU107 5.0 95.9 1.0

Zinc binding site 4 out of 17 in 6ivm

Go back to Zinc Binding Sites List in 6ivm
Zinc binding site 4 out of 17 in the Crystal Structure of A Membrane Protein P143A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of A Membrane Protein P143A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn304

b:79.8
occ:1.00
OD2 A:ASP269 2.0 74.0 1.0
OD2 A:ASP261 2.3 99.1 1.0
O A:HOH419 2.7 62.3 1.0
CG A:ASP269 2.9 71.3 1.0
OD1 A:ASP269 3.0 74.3 1.0
CG A:ASP261 3.2 90.1 1.0
CB A:ASP261 3.5 87.3 1.0
CB A:ALA266 3.5 63.6 1.0
O A:ASP261 3.9 73.5 1.0
CA A:GLY264 3.9 60.6 1.0
N A:ALA266 4.1 69.4 1.0
N A:THR265 4.3 66.7 1.0
CB A:ASP269 4.3 70.1 1.0
OD1 A:ASP261 4.4 89.3 1.0
C A:GLY264 4.4 63.3 1.0
CA A:ALA266 4.4 67.8 1.0
N A:GLY264 4.6 59.4 1.0
CA A:ASP261 4.7 83.4 1.0
C A:ASP261 4.8 73.6 1.0

Zinc binding site 5 out of 17 in 6ivm

Go back to Zinc Binding Sites List in 6ivm
Zinc binding site 5 out of 17 in the Crystal Structure of A Membrane Protein P143A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of A Membrane Protein P143A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn302

b:0.5
occ:1.00
ND1 B:HIS235 2.4 0.6 1.0
O B:HOH408 2.5 64.0 1.0
CG B:HIS235 3.1 0.6 1.0
CB B:HIS235 3.1 0.3 1.0
CA B:HIS235 3.4 0.9 1.0
CE1 B:HIS235 3.5 0.6 1.0
C B:HIS235 4.1 0.1 1.0
CD2 B:TYR42 4.1 94.4 1.0
O B:HIS235 4.3 0.5 1.0
CD2 B:HIS235 4.3 0.2 1.0
O B:HOH413 4.5 62.0 1.0
NE2 B:HIS235 4.5 0.2 1.0
CE2 B:TYR42 4.6 96.2 1.0
N B:HIS235 4.7 0.3 1.0
N B:TYR236 4.8 0.0 1.0
CG B:TYR42 4.9 92.2 1.0
CG1 B:VAL231 5.0 85.1 1.0

Zinc binding site 6 out of 17 in 6ivm

Go back to Zinc Binding Sites List in 6ivm
Zinc binding site 6 out of 17 in the Crystal Structure of A Membrane Protein P143A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Crystal Structure of A Membrane Protein P143A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn303

b:77.4
occ:1.00
CL D:CL306 2.0 81.5 1.0
NE2 B:HIS194 2.2 52.6 1.0
O D:HOH408 2.2 63.1 1.0
OE2 D:GLU191 2.5 83.7 1.0
OE1 D:GLU191 2.5 79.2 1.0
CD D:GLU191 2.9 77.2 1.0
CD2 B:HIS194 3.1 50.7 1.0
CE1 B:HIS194 3.3 53.3 1.0
NZ D:LYS188 3.6 75.0 1.0
CG B:HIS194 4.3 49.5 1.0
ND1 B:HIS194 4.3 53.0 1.0
CG D:GLU191 4.4 66.2 1.0
CD D:LYS188 4.6 63.6 1.0
CE D:LYS188 4.6 72.2 1.0
CG2 D:ILE91 4.7 50.4 1.0
CB B:ASP190 4.7 77.3 1.0

Zinc binding site 7 out of 17 in 6ivm

Go back to Zinc Binding Sites List in 6ivm
Zinc binding site 7 out of 17 in the Crystal Structure of A Membrane Protein P143A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Crystal Structure of A Membrane Protein P143A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn304

b:63.7
occ:1.00
ND1 B:HIS111 2.1 57.5 1.0
NE2 B:HIS290 2.2 90.2 1.0
ND1 B:HIS108 2.2 78.5 1.0
O B:ACY306 2.4 72.9 1.0
CE1 B:HIS111 3.0 60.5 1.0
CG B:HIS111 3.1 56.7 1.0
CD2 B:HIS290 3.1 91.2 1.0
CE1 B:HIS108 3.1 80.7 1.0
CE1 B:HIS290 3.2 92.8 1.0
C B:ACY306 3.3 88.4 1.0
CG B:HIS108 3.3 74.8 1.0
OXT B:ACY306 3.3 89.2 1.0
CB B:HIS111 3.5 54.7 1.0
CB B:HIS108 3.6 68.4 1.0
CA B:HIS108 3.7 65.7 1.0
NE2 B:HIS111 4.1 61.1 1.0
CD2 B:HIS111 4.2 58.4 1.0
O B:GLY288 4.3 0.9 1.0
NE2 B:HIS108 4.3 79.2 1.0
CG B:HIS290 4.3 95.9 1.0
ND1 B:HIS290 4.3 94.8 1.0
CD2 B:HIS108 4.4 79.0 1.0
N B:HIS108 4.5 63.0 1.0
O B:PRO105 4.7 63.5 1.0
O B:HIS108 4.7 67.8 1.0
CH3 B:ACY306 4.7 79.6 1.0
C B:HIS108 4.7 67.5 1.0
CG B:ARG101 4.7 62.8 1.0
NE B:ARG101 4.8 79.6 1.0
CA B:HIS111 5.0 57.2 1.0

Zinc binding site 8 out of 17 in 6ivm

Go back to Zinc Binding Sites List in 6ivm
Zinc binding site 8 out of 17 in the Crystal Structure of A Membrane Protein P143A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Crystal Structure of A Membrane Protein P143A within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn301

b:61.8
occ:1.00
CL C:CL304 2.0 64.0 1.0
NE2 D:HIS194 2.1 53.6 1.0
O C:HOH409 2.1 40.9 1.0
OE2 C:GLU191 2.3 67.3 1.0
OE1 C:GLU191 2.4 62.9 1.0
CD C:GLU191 2.7 65.6 1.0
CD2 D:HIS194 3.0 55.0 1.0
CE1 D:HIS194 3.2 56.8 1.0
NZ C:LYS188 3.7 63.9 1.0
CG D:HIS194 4.2 54.9 1.0
CG C:GLU191 4.2 60.7 1.0
ND1 D:HIS194 4.2 56.9 1.0
CG2 C:ILE91 4.4 48.4 1.0
CD C:LYS188 4.8 54.4 1.0
CE C:LYS188 4.9 57.9 1.0
CB D:ASP190 5.0 70.6 1.0
O D:ASP190 5.0 55.7 1.0

Zinc binding site 9 out of 17 in 6ivm

Go back to Zinc Binding Sites List in 6ivm
Zinc binding site 9 out of 17 in the Crystal Structure of A Membrane Protein P143A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Crystal Structure of A Membrane Protein P143A within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn302

b:78.1
occ:1.00
CL E:CL305 2.1 98.4 1.0
NE2 C:HIS194 2.1 45.2 1.0
OE1 E:GLU191 2.2 64.8 1.0
O C:HOH407 2.7 59.6 1.0
OD1 C:ASP190 2.8 84.2 1.0
CD E:GLU191 2.9 65.7 1.0
OE2 E:GLU191 2.9 70.8 1.0
CD2 C:HIS194 3.0 47.0 1.0
CE1 C:HIS194 3.2 45.2 1.0
CG C:ASP190 3.8 78.4 1.0
CE E:LYS188 4.0 60.6 1.0
OD2 C:ASP190 4.0 91.1 1.0
CG C:HIS194 4.2 45.9 1.0
CG E:GLU191 4.2 57.8 1.0
ND1 C:HIS194 4.3 46.3 1.0
CD E:LYS188 4.7 57.6 1.0
NZ E:LYS188 4.8 62.4 1.0
CG2 E:ILE91 4.8 41.7 1.0

Zinc binding site 10 out of 17 in 6ivm

Go back to Zinc Binding Sites List in 6ivm
Zinc binding site 10 out of 17 in the Crystal Structure of A Membrane Protein P143A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Crystal Structure of A Membrane Protein P143A within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn303

b:67.9
occ:1.00
ND1 C:HIS108 1.9 62.8 1.0
ND1 C:HIS111 2.0 66.5 1.0
CL C:CL305 2.3 83.6 1.0
O C:HOH408 2.3 61.6 1.0
CE1 C:HIS111 2.9 65.8 1.0
CE1 C:HIS108 2.9 63.3 1.0
CG C:HIS108 2.9 64.4 1.0
CG C:HIS111 3.1 65.4 1.0
CB C:HIS108 3.3 67.3 1.0
CB C:HIS111 3.5 64.4 1.0
CA C:HIS108 3.6 72.0 1.0
NE2 C:HIS111 4.0 66.3 1.0
NE2 C:HIS108 4.0 66.1 1.0
CD2 C:HIS108 4.1 63.6 1.0
CD2 C:HIS111 4.1 64.2 1.0
NE C:ARG101 4.3 83.9 1.0
N C:HIS108 4.4 75.6 1.0
O C:PRO105 4.6 72.8 1.0
O C:HIS108 4.6 70.0 1.0
NH1 C:ARG101 4.6 90.0 1.0
C C:HIS108 4.7 72.9 1.0
CZ C:ARG101 4.8 82.9 1.0
CA C:HIS111 5.0 63.5 1.0

Reference:

C.Ji, A.Kittredge, A.Hopiavuori, N.Ward, S.Chen, Y.Fukuda, Y.Zhang, T.Yang. Dual CA2+-Dependent Gates in Human BESTROPHIN1 Underlie Disease-Causing Mechanisms of Gain-of-Function Mutations. Commun Biol V. 2 240 2019.
ISSN: ESSN 2399-3642
PubMed: 31263784
DOI: 10.1038/S42003-019-0433-3
Page generated: Tue Oct 29 00:22:50 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy