Atomistry » Calcium » PDB 4wnb-4x8d » 4wp9
Atomistry »
  Calcium »
    PDB 4wnb-4x8d »
      4wp9 »

Calcium in PDB 4wp9: Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to 2'5'-Dd-3'-Atp, Calcium and Magnesium Ion

Enzymatic activity of Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to 2'5'-Dd-3'-Atp, Calcium and Magnesium Ion

All present enzymatic activity of Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to 2'5'-Dd-3'-Atp, Calcium and Magnesium Ion:
4.6.1.1;

Protein crystallography data

The structure of Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to 2'5'-Dd-3'-Atp, Calcium and Magnesium Ion, PDB code: 4wp9 was solved by N.G.Bharambe, D.V.Barathy, K.Suguna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.95 / 1.38
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 52.470, 56.090, 55.770, 90.00, 110.72, 90.00
R / Rfree (%) 23.1 / 26.4

Other elements in 4wp9:

The structure of Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to 2'5'-Dd-3'-Atp, Calcium and Magnesium Ion also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to 2'5'-Dd-3'-Atp, Calcium and Magnesium Ion (pdb code 4wp9). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to 2'5'-Dd-3'-Atp, Calcium and Magnesium Ion, PDB code: 4wp9:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in 4wp9

Go back to Calcium Binding Sites List in 4wp9
Calcium binding site 1 out of 3 in the Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to 2'5'-Dd-3'-Atp, Calcium and Magnesium Ion


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to 2'5'-Dd-3'-Atp, Calcium and Magnesium Ion within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca304

b:16.9
occ:1.00
 O2B A:ZDA303 2.2 18.0 1.0
OD1 A:ASP61 2.3 20.1 1.0
O2A A:ZDA303 2.3 17.1 1.0
OD2 A:ASP105 2.3 20.5 1.0
O A:ILE62 2.3 15.9 1.0
O3G A:ZDA303 2.3 20.5 1.0
OD2 A:ASP61 2.8 21.5 1.0
CG A:ASP61 2.8 18.7 1.0
PB A:ZDA303 3.3 16.9 1.0
CG A:ASP105 3.3 17.0 1.0
PA A:ZDA303 3.4 19.4 1.0
C A:ILE62 3.5 14.1 1.0
MG A:MG302 3.5 27.1 1.0
PG A:ZDA303 3.5 21.6 1.0
O3A A:ZDA303 3.7 20.4 1.0
O3B A:ZDA303 3.7 16.0 1.0
H A:SER65 3.7 20.2 1.0
OD1 A:ASP105 3.8 19.8 1.0
HG A:SER65 3.9 19.0 1.0
H A:ILE62 3.9 19.4 1.0
OG A:SER65 4.0 15.8 1.0
N A:ILE62 4.0 16.2 1.0
O A:HOH416 4.1 30.1 1.0
HA A:GLU63 4.1 22.5 1.0
HB3 A:SER65 4.2 19.2 1.0
H A:GLU64 4.2 22.3 1.0
HH11 A:ARG143 4.2 34.1 1.0
HB A:ILE62 4.3 18.7 1.0
CA A:ILE62 4.3 15.4 1.0
CB A:ASP61 4.3 16.9 1.0
O A:HOH448 4.4 27.7 1.0
O2G A:ZDA303 4.4 24.9 1.0
C A:ASP61 4.4 15.5 1.0
O3' A:ZDA303 4.5 24.4 1.0
N A:GLU63 4.5 15.9 1.0
HB2 A:ASP105 4.5 22.0 1.0
N A:GLU64 4.6 18.6 1.0
CB A:ASP105 4.6 18.3 1.0
HH12 A:ARG143 4.6 34.1 1.0
N A:SER65 4.6 16.9 1.0
CB A:SER65 4.6 16.0 1.0
O1A A:ZDA303 4.6 23.6 1.0
O1G A:ZDA303 4.6 23.1 1.0
CA A:GLU63 4.6 18.8 1.0
H12 A:ZDA303 4.6 26.9 1.0
HA A:ASP61 4.7 18.6 1.0
HB2 A:ASP61 4.7 20.3 1.0
O1B A:ZDA303 4.7 20.0 1.0
NH1 A:ARG143 4.7 28.4 1.0
CA A:ASP61 4.8 15.5 1.0
CB A:ILE62 4.8 15.6 1.0
HB3 A:ASP61 4.8 20.3 1.0
C A:GLU63 4.8 18.6 1.0
HG22 A:ILE62 4.9 18.8 1.0
C3' A:ZDA303 5.0 22.4 1.0
HB3 A:ASP105 5.0 22.0 1.0

Calcium binding site 2 out of 3 in 4wp9

Go back to Calcium Binding Sites List in 4wp9
Calcium binding site 2 out of 3 in the Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to 2'5'-Dd-3'-Atp, Calcium and Magnesium Ion


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to 2'5'-Dd-3'-Atp, Calcium and Magnesium Ion within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca305

b:25.4
occ:1.00
 HE21 A:GLN172 2.0 71.5 1.0
HE A:ARG168 2.1 43.3 1.0
HE22 A:GLN172 2.2 71.5 1.0
NE2 A:GLN172 2.3 59.6 1.0
NH2 A:ARG168 2.5 46.5 1.0
HA A:LEU204 2.8 25.3 1.0
NE A:ARG168 2.8 36.1 1.0
CZ A:ARG168 3.1 44.2 1.0
HB3 A:ARG168 3.1 23.5 1.0
N A:LYS205 3.2 22.5 1.0
HH22 A:ARG168 3.2 55.8 1.0
HD23 A:LEU204 3.5 26.2 1.0
HB2 A:LYS205 3.5 28.2 1.0
CD A:GLN172 3.6 41.3 1.0
HD22 A:LEU204 3.6 26.2 1.0
CA A:LEU204 3.7 21.1 1.0
HB3 A:LEU204 3.9 23.8 1.0
O A:HOH406 3.9 32.0 1.0
HB3 A:LYS205 3.9 28.2 1.0
HG2 A:GLN172 3.9 30.2 1.0
C A:LEU204 3.9 23.7 1.0
CD2 A:LEU204 4.0 21.8 1.0
CB A:ARG168 4.0 19.6 1.0
CB A:LYS205 4.0 23.5 1.0
CD A:ARG168 4.1 29.6 1.0
O A:GLU203 4.1 26.2 1.0
HG3 A:ARG168 4.2 27.3 1.0
CA A:LYS205 4.2 23.8 1.0
CB A:LEU204 4.2 19.8 1.0
HB3 A:ALA171 4.3 22.4 1.0
O A:ARG168 4.3 16.5 1.0
CG A:ARG168 4.3 22.7 1.0
CG A:GLN172 4.3 25.1 1.0
HA A:ARG168 4.3 20.5 1.0
NH1 A:ARG168 4.4 45.7 1.0
OE1 A:GLN172 4.4 34.3 1.0
HD3 A:ARG168 4.6 35.5 1.0
CA A:ARG168 4.6 17.1 1.0
HD2 A:ARG168 4.7 35.5 1.0
HB2 A:ARG168 4.7 23.5 1.0
HG3 A:GLN172 4.7 30.2 1.0
HA A:LYS205 4.8 28.5 1.0
HD21 A:LEU204 4.8 26.2 1.0
N A:LEU204 4.8 19.9 1.0
CG A:LEU204 4.8 22.2 1.0
C A:ARG168 4.8 15.1 1.0
HH12 A:ARG168 4.8 54.9 1.0
C A:GLU203 4.9 23.5 1.0
HH11 A:ARG168 4.9 54.9 1.0

Calcium binding site 3 out of 3 in 4wp9

Go back to Calcium Binding Sites List in 4wp9
Calcium binding site 3 out of 3 in the Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to 2'5'-Dd-3'-Atp, Calcium and Magnesium Ion


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of Adenylyl Cyclase MA1120 From Mycobacterium Avium Bound to 2'5'-Dd-3'-Atp, Calcium and Magnesium Ion within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca303

b:15.6
occ:1.00
 OD1 B:ASP61 2.2 16.1 1.0
O B:ILE62 2.3 17.5 1.0
O3G B:ZDA301 2.3 15.7 1.0
O1B B:ZDA301 2.3 16.7 1.0
OD2 B:ASP105 2.3 19.1 1.0
O1A B:ZDA301 2.4 18.0 1.0
CG B:ASP61 3.4 17.6 1.0
PB B:ZDA301 3.4 15.5 1.0
CG B:ASP105 3.4 19.3 1.0
C B:ILE62 3.4 16.0 1.0
PG B:ZDA301 3.5 16.4 1.0
PA B:ZDA301 3.5 18.1 1.0
O3B B:ZDA301 3.7 13.6 1.0
O3A B:ZDA301 3.8 16.4 1.0
HH22 B:ARG143 3.8 25.9 1.0
H B:SER65 3.8 20.3 1.0
OD1 B:ASP105 3.8 20.0 1.0
H12 B:ZDA301 3.8 23.8 1.0
H B:ILE62 3.9 16.8 1.0
HE21 B:GLN103 3.9 26.8 1.0
N B:ILE62 3.9 14.0 1.0
HE22 B:GLN103 3.9 26.8 1.0
OD2 B:ASP61 3.9 23.0 1.0
HG B:SER65 4.0 22.9 1.0
MG B:MG302 4.0 28.7 1.0
HB3 B:SER65 4.1 24.2 1.0
OG B:SER65 4.1 19.1 1.0
NH1 B:ARG143 4.2 22.5 1.0
CA B:ILE62 4.2 16.1 1.0
H B:GLU64 4.2 20.1 1.0
HB B:ILE62 4.2 20.6 1.0
NE2 B:GLN103 4.3 22.4 1.0
O1G B:ZDA301 4.3 18.6 1.0
HA B:GLU63 4.3 21.0 1.0
C B:ASP61 4.3 15.3 1.0
NH2 B:ARG143 4.4 21.6 1.0
N B:GLU63 4.5 16.3 1.0
CB B:ASP61 4.5 15.0 1.0
HA B:ASP61 4.5 17.3 1.0
N B:GLU64 4.6 16.7 1.0
HB2 B:ASP105 4.6 23.1 1.0
CB B:SER65 4.6 20.2 1.0
HB3 B:ASP61 4.6 18.0 1.0
O2G B:ZDA301 4.6 18.3 1.0
N B:SER65 4.6 16.9 1.0
O3' B:ZDA301 4.7 20.4 1.0
CB B:ASP105 4.7 19.3 1.0
CZ B:ARG143 4.7 20.3 1.0
C3' B:ZDA301 4.7 19.8 1.0
HH11 B:ARG143 4.7 27.0 1.0
O2A B:ZDA301 4.7 17.4 1.0
CA B:ASP61 4.7 14.4 1.0
CA B:GLU63 4.7 17.5 1.0
CB B:ILE62 4.7 17.1 1.0
HG22 B:ILE62 4.8 22.0 1.0
O2B B:ZDA301 4.8 16.9 1.0
C B:GLU63 4.8 17.9 1.0
O B:ASP61 4.9 16.8 1.0
HH21 B:ARG143 5.0 25.9 1.0

Reference:

D.V.Barathy, N.G.Bharambe, W.Syed, A.Zaveri, S.S.Visweswariah, M.Cola Sigmaf O, S.Misquith, K.Suguna. Autoinhibitory Mechanism and Activity-Related Structural Changes in A Mycobacterial Adenylyl Cyclase J.Struct.Biol. V. 190 304 2015.
ISSN: ESSN 1095-8657
PubMed: 25916753
DOI: 10.1016/J.JSB.2015.04.013
Page generated: Sun Jul 14 14:20:26 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy