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Magnesium in PDB 4wzb: Crystal Structure of Mgamppcp-Bound AV2-AV1 Complex

Enzymatic activity of Crystal Structure of Mgamppcp-Bound AV2-AV1 Complex

All present enzymatic activity of Crystal Structure of Mgamppcp-Bound AV2-AV1 Complex:
1.18.6.1;

Protein crystallography data

The structure of Crystal Structure of Mgamppcp-Bound AV2-AV1 Complex, PDB code: 4wzb was solved by F.A.Tezcan, J.T.Kaiser, D.Mustafi, M.Y.Walton, J.B.Howard, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.38 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 110.533, 120.894, 264.834, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 25.5

Other elements in 4wzb:

The structure of Crystal Structure of Mgamppcp-Bound AV2-AV1 Complex also contains other interesting chemical elements:

Molybdenum (Mo) 2 atoms
Iron (Fe) 40 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Mgamppcp-Bound AV2-AV1 Complex (pdb code 4wzb). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of Mgamppcp-Bound AV2-AV1 Complex, PDB code: 4wzb:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 4wzb

Go back to Magnesium Binding Sites List in 4wzb
Magnesium binding site 1 out of 4 in the Crystal Structure of Mgamppcp-Bound AV2-AV1 Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Mgamppcp-Bound AV2-AV1 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg1291

b:40.3
occ:1.00
OG E:SER16 1.9 37.2 1.0
O E:HOH1302 1.9 38.8 1.0
O2B E:ACP1292 2.1 38.5 1.0
O1G E:ACP1292 2.3 37.2 1.0
O E:HOH1322 2.3 40.3 1.0
CB E:SER16 3.0 40.1 1.0
O E:HOH1323 3.1 43.2 1.0
PB E:ACP1292 3.2 39.2 1.0
C3B E:ACP1292 3.4 38.7 1.0
PG E:ACP1292 3.5 43.6 1.0
OD2 E:ASP43 3.8 39.5 1.0
N E:SER16 3.8 39.8 1.0
O2A E:ACP1292 3.9 41.8 1.0
CA E:SER16 4.0 39.6 1.0
OD1 E:ASP43 4.0 42.0 1.0
OD2 E:ASP125 4.1 43.5 1.0
OD2 E:ASP39 4.2 47.4 1.0
CG E:ASP43 4.2 41.8 1.0
O1B E:ACP1292 4.3 39.8 1.0
O3A E:ACP1292 4.3 40.2 1.0
O3G E:ACP1292 4.4 44.3 1.0
PA E:ACP1292 4.4 39.3 1.0
OD1 E:ASP125 4.5 41.0 1.0
O2G E:ACP1292 4.5 42.7 1.0
O1A E:ACP1292 4.6 41.8 1.0
CG E:ASP125 4.7 42.6 1.0
CB E:LYS15 4.9 42.1 1.0
C E:LYS15 5.0 40.8 1.0

Magnesium binding site 2 out of 4 in 4wzb

Go back to Magnesium Binding Sites List in 4wzb
Magnesium binding site 2 out of 4 in the Crystal Structure of Mgamppcp-Bound AV2-AV1 Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Mgamppcp-Bound AV2-AV1 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg1291

b:41.8
occ:1.00
O F:HOH1304 1.9 40.7 1.0
OG F:SER16 2.0 37.3 1.0
O2G F:ACP1292 2.0 38.9 1.0
O F:HOH1305 2.1 40.0 1.0
O F:HOH1306 2.3 39.6 1.0
O1B F:ACP1292 2.4 39.5 1.0
CB F:SER16 3.3 39.1 1.0
PG F:ACP1292 3.5 38.3 1.0
PB F:ACP1292 3.6 35.0 1.0
OD1 F:ASP125 3.6 41.2 1.0
C3B F:ACP1292 4.0 41.2 1.0
N F:SER16 4.1 38.5 1.0
OD2 F:ASP39 4.2 43.0 1.0
CA F:SER16 4.2 38.4 1.0
O3G F:ACP1292 4.3 37.0 1.0
OD2 F:ASP125 4.3 39.6 1.0
OD1 F:ASP43 4.3 45.2 1.0
OD2 F:ASP43 4.3 48.4 1.0
O2B F:ACP1292 4.4 35.4 1.0
CG F:ASP125 4.4 38.0 1.0
CE F:LYS41 4.4 43.1 1.0
NZ F:LYS41 4.5 41.4 1.0
CE F:LYS15 4.5 37.6 1.0
O F:VAL126 4.5 40.5 1.0
O1G F:ACP1292 4.6 45.4 1.0
O1A F:ACP1292 4.7 43.6 1.0
CB F:LYS15 4.7 38.5 1.0
CG F:ASP43 4.7 45.6 1.0
O3A F:ACP1292 4.8 44.4 1.0
O2A F:ACP1292 5.0 42.0 1.0

Magnesium binding site 3 out of 4 in 4wzb

Go back to Magnesium Binding Sites List in 4wzb
Magnesium binding site 3 out of 4 in the Crystal Structure of Mgamppcp-Bound AV2-AV1 Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Mgamppcp-Bound AV2-AV1 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mg1291

b:35.0
occ:1.00
O G:HOH1312 1.8 33.1 1.0
O1G G:ACP1290 1.9 35.2 1.0
O G:HOH1354 2.0 33.4 1.0
OG G:SER16 2.2 33.3 1.0
O G:HOH1313 2.4 33.5 1.0
O2B G:ACP1290 2.5 35.5 1.0
PG G:ACP1290 3.4 37.5 1.0
NZ G:LYS15 3.5 37.5 1.0
CB G:SER16 3.6 33.9 1.0
PB G:ACP1290 3.7 33.5 1.0
OD2 G:ASP125 3.8 36.4 1.0
OD2 G:ASP39 3.9 43.2 1.0
C3B G:ACP1290 3.9 36.3 1.0
N G:SER16 4.2 31.9 1.0
O3G G:ACP1290 4.3 42.9 1.0
O2G G:ACP1290 4.3 33.9 1.0
OD1 G:ASP125 4.3 33.4 1.0
OD2 G:ASP43 4.3 37.1 1.0
NZ G:LYS41 4.3 39.3 1.0
CA G:SER16 4.4 33.9 1.0
OD1 G:ASP43 4.4 43.4 1.0
CG G:ASP125 4.5 34.4 1.0
O1B G:ACP1290 4.5 29.9 1.0
O2A G:ACP1290 4.6 36.6 1.0
CE G:LYS41 4.7 39.4 1.0
CG G:ASP43 4.8 42.7 1.0
CB G:LYS15 4.8 31.1 1.0
O3A G:ACP1290 4.9 33.3 1.0
CG G:ASP39 4.9 39.6 1.0
CE G:LYS15 5.0 36.3 1.0

Magnesium binding site 4 out of 4 in 4wzb

Go back to Magnesium Binding Sites List in 4wzb
Magnesium binding site 4 out of 4 in the Crystal Structure of Mgamppcp-Bound AV2-AV1 Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Mgamppcp-Bound AV2-AV1 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mg1291

b:25.5
occ:1.00
O2G H:ACP1292 1.8 28.8 1.0
OG H:SER16 2.1 26.4 1.0
O H:HOH1307 2.1 29.8 1.0
O H:HOH1362 2.2 22.8 1.0
O H:HOH1308 2.3 27.4 1.0
O1B H:ACP1292 2.3 26.4 1.0
PG H:ACP1292 3.3 26.2 1.0
CB H:SER16 3.4 27.5 1.0
PB H:ACP1292 3.5 25.9 1.0
NZ H:LYS15 3.6 27.7 1.0
NZ H:LYS41 3.8 33.6 1.0
C3B H:ACP1292 3.8 30.4 1.0
OD2 H:ASP39 3.9 32.7 1.0
OD2 H:ASP125 4.0 28.5 1.0
N H:SER16 4.1 24.9 1.0
OD2 H:ASP43 4.1 27.2 1.0
OD1 H:ASP43 4.1 31.0 1.0
O3G H:ACP1292 4.1 26.0 1.0
OD1 H:ASP125 4.3 30.7 1.0
CA H:SER16 4.3 26.1 1.0
O1G H:ACP1292 4.4 35.0 1.0
O2B H:ACP1292 4.5 22.7 1.0
CG H:ASP43 4.5 30.9 1.0
CG H:ASP125 4.5 29.6 1.0
O1A H:ACP1292 4.6 25.9 1.0
O H:VAL126 4.7 33.6 1.0
O3A H:ACP1292 4.7 28.6 1.0
CB H:LYS15 4.8 26.9 1.0
CG H:ASP39 4.9 32.1 1.0
CE H:LYS41 4.9 29.2 1.0
PA H:ACP1292 5.0 28.6 1.0

Reference:

F.A.Tezcan, J.T.Kaiser, D.Mustafi, M.Y.Walton, J.B.Howard, D.C.Rees. Nitrogenase Complexes: Multiple Docking Sites For A Nucleotide Switch Protein. Science V. 309 1377 2005.
ISSN: ESSN 1095-9203
PubMed: 16123301
DOI: 10.1126/SCIENCE.1115653
Page generated: Tue Aug 20 14:01:35 2024

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