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Manganese in PDB 8vh8: Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A

Protein crystallography data

The structure of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A, PDB code: 8vh8 was solved by L.C.Pedersen, J.Liu, E.Stancanelli, J.M.Krahn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.76 / 2.85
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 118.57, 118.57, 262.356, 90, 90, 90
R / Rfree (%) 19.8 / 22.3

Other elements in 8vh8:

The structure of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A also contains other interesting chemical elements:

Sodium (Na) 4 atoms
Calcium (Ca) 1 atom
Chlorine (Cl) 18 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A (pdb code 8vh8). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 8 binding sites of Manganese where determined in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A, PDB code: 8vh8:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Manganese binding site 1 out of 8 in 8vh8

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Manganese binding site 1 out of 8 in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn701

b:110.9
occ:1.00
OD2 A:ASP481 2.1 114.8 1.0
O2A A:UDP702 2.1 111.4 1.0
O1B A:UDP702 2.2 110.4 1.0
O A:HOH801 2.2 105.0 1.0
CG A:ASP481 3.0 112.4 1.0
OD1 A:ASP481 3.3 109.4 1.0
PB A:UDP702 3.3 110.7 1.0
PA A:UDP702 3.4 111.4 1.0
O3A A:UDP702 3.5 110.6 1.0
O3B A:UDP702 3.9 109.8 1.0
H5'1 A:UDP702 3.9 132.7 1.0
HH22 A:ARG403 4.0 137.3 1.0
HH12 A:ARG403 4.1 137.4 1.0
OD2 A:ASP479 4.3 98.5 1.0
O1A A:UDP702 4.3 111.6 1.0
CB A:ASP481 4.4 112.4 1.0
O5' A:UDP702 4.5 111.3 1.0
O2B A:UDP702 4.6 110.8 1.0
C5' A:UDP702 4.6 110.5 1.0
HB2 A:ASP481 4.6 134.9 1.0
NH2 A:ARG403 4.7 114.4 1.0
HB3 A:ASP479 4.7 118.0 1.0
HB3 A:ASP481 4.7 134.9 1.0
H5'2 A:UDP702 4.8 132.7 1.0
NH1 A:ARG403 4.8 114.5 1.0

Manganese binding site 2 out of 8 in 8vh8

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Manganese binding site 2 out of 8 in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn703

b:72.0
occ:1.00
O3B A:UDP704 2.1 73.4 1.0
OD2 A:ASP217 2.1 70.2 1.0
O A:HOH802 2.2 73.5 1.0
OD1 A:ASP217 2.2 68.4 1.0
O2A A:UDP704 2.3 70.2 1.0
CG A:ASP217 2.5 68.7 1.0
H5'1 A:UDP704 3.1 81.2 1.0
PB A:UDP704 3.2 73.4 1.0
O3A A:UDP704 3.3 71.1 1.0
PA A:UDP704 3.3 70.4 1.0
HH12 A:ARG247 3.6 95.4 1.0
OD1 A:ASP218 3.6 74.6 1.0
OD1 A:ASN317 3.8 78.8 1.0
H3' A:UDP704 3.8 78.9 1.0
HE A:ARG320 3.8 86.3 1.0
OD2 A:ASP218 3.8 71.2 1.0
CB A:ASP217 4.0 66.5 1.0
O1B A:UDP704 4.0 74.2 1.0
C5' A:UDP704 4.1 67.6 1.0
CG A:ASP218 4.1 73.0 1.0
O5' A:UDP704 4.2 67.3 1.0
HB3 A:ASP215 4.2 77.6 1.0
HH21 A:ARG320 4.3 83.7 1.0
HB3 A:ASP217 4.3 79.8 1.0
HB2 A:ASP215 4.3 77.6 1.0
O A:THR318 4.4 79.9 1.0
HB2 A:ASP217 4.4 79.8 1.0
NH1 A:ARG247 4.4 79.5 1.0
O2B A:UDP704 4.4 76.7 1.0
HB2 A:SER323 4.5 98.3 1.0
OD2 A:ASP215 4.6 66.7 1.0
HH22 A:ARG247 4.6 94.4 1.0
O1A A:UDP704 4.6 71.8 1.0
H A:ASP217 4.6 75.9 1.0
NE A:ARG320 4.6 71.9 1.0
CB A:ASP215 4.7 64.7 1.0
H5'2 A:UDP704 4.7 81.2 1.0
C3' A:UDP704 4.8 65.8 1.0
HH11 A:ARG247 4.8 95.4 1.0
HG2 A:ARG320 4.8 94.7 1.0
H A:THR318 4.9 92.1 1.0
CA A:ASP217 5.0 64.2 1.0
C4' A:UDP704 5.0 65.2 1.0
HB A:THR318 5.0 91.1 1.0
CG A:ASN317 5.0 79.0 1.0

Manganese binding site 3 out of 8 in 8vh8

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Manganese binding site 3 out of 8 in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn701

b:97.6
occ:1.00
O1B B:UDP702 2.1 94.8 1.0
O B:HOH802 2.1 91.0 1.0
OD2 B:ASP481 2.2 98.5 1.0
O2A B:UDP702 2.2 94.1 1.0
CG B:ASP481 3.1 94.3 1.0
PA B:UDP702 3.3 94.3 1.0
PB B:UDP702 3.4 95.0 1.0
OD1 B:ASP481 3.4 90.8 1.0
O3A B:UDP702 3.5 94.0 1.0
O3B B:UDP702 4.3 94.2 1.0
O1A B:UDP702 4.3 94.4 1.0
O2B B:UDP702 4.4 94.8 1.0
OD2 B:ASP479 4.4 88.6 1.0
CB B:ASP481 4.5 96.3 1.0
O5' B:UDP702 4.5 93.5 1.0
OE2 B:GLU595 4.5 107.7 1.0
OD1 B:ASN597 4.6 121.0 1.0
H5'1 B:UDP702 4.6 111.6 1.0
HB2 B:ASP481 4.6 115.5 1.0
HB3 B:ASP481 4.7 115.5 1.0
HB3 B:ASP479 4.8 103.0 1.0
HG3 B:GLU595 4.9 122.3 1.0

Manganese binding site 4 out of 8 in 8vh8

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Manganese binding site 4 out of 8 in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn703

b:68.2
occ:1.00
O3B B:UDP704 2.1 69.8 1.0
OD2 B:ASP217 2.1 66.9 1.0
O2A B:UDP704 2.2 65.8 1.0
O B:HOH801 2.2 72.8 1.0
OD1 B:ASP217 2.3 63.4 1.0
CG B:ASP217 2.5 64.0 1.0
H5'1 B:UDP704 3.1 73.5 1.0
PB B:UDP704 3.2 69.9 1.0
PA B:UDP704 3.3 66.0 1.0
O3A B:UDP704 3.3 66.2 1.0
HH12 B:ARG247 3.5 91.1 1.0
HE B:ARG320 3.6 80.7 1.0
H3' B:UDP704 3.7 71.7 1.0
OD1 B:ASP218 3.8 68.0 1.0
OD2 B:ASP218 3.8 64.7 1.0
O1B B:UDP704 3.9 68.8 1.0
HH21 B:ARG320 3.9 78.0 1.0
OD1 B:ASN317 4.0 76.2 1.0
C5' B:UDP704 4.0 61.3 1.0
CB B:ASP217 4.0 61.3 1.0
HB3 B:ASP215 4.1 71.5 1.0
O5' B:UDP704 4.1 62.0 1.0
CG B:ASP218 4.2 65.3 1.0
HB2 B:ASP215 4.2 71.5 1.0
HB3 B:ASP217 4.3 73.6 1.0
NH1 B:ARG247 4.3 75.9 1.0
OD2 B:ASP215 4.3 61.2 1.0
HB2 B:SER323 4.4 93.0 1.0
O B:THR318 4.4 77.8 1.0
HB2 B:ASP217 4.4 73.6 1.0
HH22 B:ARG247 4.4 88.6 1.0
NE B:ARG320 4.4 67.2 1.0
O2B B:UDP704 4.5 71.8 1.0
O1A B:UDP704 4.5 67.3 1.0
CB B:ASP215 4.6 59.6 1.0
H B:ASP217 4.6 70.2 1.0
H5'2 B:UDP704 4.7 73.5 1.0
NH2 B:ARG320 4.7 65.0 1.0
HH11 B:ARG247 4.7 91.1 1.0
C3' B:UDP704 4.7 59.8 1.0
HG2 B:ARG320 4.8 91.5 1.0
HB B:THR318 4.8 88.5 1.0
H B:THR318 4.9 90.7 1.0
CG B:ASP215 4.9 60.2 1.0
C4' B:UDP704 4.9 59.4 1.0

Manganese binding site 5 out of 8 in 8vh8

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Manganese binding site 5 out of 8 in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn701

b:105.9
occ:1.00
O C:HOH801 2.1 101.4 1.0
O2A C:UDP702 2.2 105.5 1.0
OD2 C:ASP481 2.2 101.3 1.0
O1B C:UDP702 2.4 105.1 1.0
CG C:ASP481 3.0 99.4 1.0
OD1 C:ASP481 3.1 98.6 1.0
PA C:UDP702 3.4 106.7 1.0
PB C:UDP702 3.4 106.9 1.0
O3A C:UDP702 3.5 106.1 1.0
HH22 C:ARG403 3.8 133.4 1.0
HH12 C:ARG403 3.8 127.8 1.0
O3B C:UDP702 3.9 105.4 1.0
H5'1 C:UDP702 4.0 127.2 1.0
OD2 C:ASP479 4.1 102.0 1.0
O5' C:UDP702 4.4 106.4 1.0
O1A C:UDP702 4.4 106.6 1.0
CB C:ASP481 4.4 98.6 1.0
NH2 C:ARG403 4.5 111.1 1.0
NH1 C:ARG403 4.5 106.5 1.0
HB3 C:ASP479 4.5 118.3 1.0
HB2 C:ASP481 4.7 118.3 1.0
O2B C:UDP702 4.7 105.5 1.0
C5' C:UDP702 4.7 106.0 1.0
HB3 C:ASP481 4.8 118.3 1.0
H3' C:UDP702 4.9 125.8 1.0
HD11 C:ILE482 4.9 106.0 1.0
CZ C:ARG403 4.9 110.1 1.0
HG13 C:ILE482 4.9 104.8 1.0
CG C:ASP479 5.0 99.8 1.0

Manganese binding site 6 out of 8 in 8vh8

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Manganese binding site 6 out of 8 in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn703

b:74.5
occ:1.00
O C:HOH802 2.1 73.7 1.0
OD2 C:ASP217 2.1 74.5 1.0
O3B C:UDP704 2.1 75.2 1.0
OD1 C:ASP217 2.2 72.6 1.0
O2A C:UDP704 2.3 70.4 1.0
CG C:ASP217 2.5 73.5 1.0
O3A C:UDP704 3.3 71.6 1.0
PB C:UDP704 3.3 75.8 1.0
PA C:UDP704 3.3 68.1 1.0
H5'1 C:UDP704 3.3 79.6 1.0
HH12 C:ARG247 3.6 93.4 1.0
OD1 C:ASP218 3.8 71.5 1.0
OD2 C:ASP218 3.8 69.3 1.0
H3' C:UDP704 3.8 77.0 1.0
OD1 C:ASN317 3.9 73.4 1.0
HE C:ARG320 3.9 84.1 1.0
CB C:ASP217 4.0 71.1 1.0
HB3 C:ASP215 4.1 78.6 1.0
O1B C:UDP704 4.1 76.4 1.0
CG C:ASP218 4.2 70.0 1.0
HB2 C:ASP215 4.2 78.6 1.0
HB3 C:ASP217 4.2 85.3 1.0
C5' C:UDP704 4.3 66.3 1.0
O5' C:UDP704 4.3 66.9 1.0
NH1 C:ARG247 4.4 77.8 1.0
O C:THR318 4.4 79.1 1.0
HB2 C:ASP217 4.4 85.3 1.0
O2B C:UDP704 4.4 77.9 1.0
OD2 C:ASP215 4.4 65.3 1.0
HH21 C:ARG320 4.4 81.2 1.0
O1A C:UDP704 4.5 72.2 1.0
H C:ASP217 4.5 82.7 1.0
HH22 C:ARG247 4.6 94.8 1.0
CB C:ASP215 4.6 65.5 1.0
H C:THR318 4.7 90.1 1.0
HH11 C:ARG247 4.7 93.4 1.0
NE C:ARG320 4.8 70.1 1.0
HB2 C:SER323 4.8 100.0 1.0
HB C:THR318 4.8 93.1 1.0
C3' C:UDP704 4.9 64.2 1.0
HG2 C:ARG320 5.0 92.3 1.0
CG C:ASP215 5.0 64.9 1.0
CA C:ASP217 5.0 69.7 1.0
H5'2 C:UDP704 5.0 79.6 1.0

Manganese binding site 7 out of 8 in 8vh8

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Manganese binding site 7 out of 8 in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 7 of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn701

b:81.0
occ:1.00
O1B D:UDP702 2.1 81.2 1.0
OD2 D:ASP481 2.2 76.8 1.0
O D:HOH802 2.2 73.8 1.0
O2A D:UDP702 2.4 80.6 1.0
CG D:ASP481 3.1 75.5 1.0
OD1 D:ASP481 3.4 74.0 1.0
PB D:UDP702 3.4 83.3 1.0
PA D:UDP702 3.5 81.5 1.0
O3A D:UDP702 3.6 81.3 1.0
HH22 D:ARG403 3.7 98.0 1.0
H5'1 D:UDP702 3.9 94.5 1.0
HH12 D:ARG403 4.0 94.1 1.0
O3B D:UDP702 4.0 84.3 1.0
OD2 D:ASP479 4.4 70.9 1.0
NH2 D:ARG403 4.4 81.7 1.0
CB D:ASP481 4.5 77.4 1.0
O1A D:UDP702 4.6 82.5 1.0
NH1 D:ARG403 4.6 78.4 1.0
O2B D:UDP702 4.6 83.1 1.0
O5' D:UDP702 4.6 80.0 1.0
HB2 D:ASP481 4.6 92.9 1.0
C5' D:UDP702 4.7 78.8 1.0
HB3 D:ASP481 4.7 92.9 1.0
HB3 D:ASP479 4.8 82.4 1.0
CZ D:ARG403 4.9 80.5 1.0
HH21 D:ARG403 4.9 98.0 1.0

Manganese binding site 8 out of 8 in 8vh8

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Manganese binding site 8 out of 8 in the Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 8 of Crystal Structure of Heparosan Synthase 2 From Pasteurella Multocida at 2.85 A within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn703

b:66.1
occ:1.00
O D:HOH801 2.0 66.0 1.0
O3B D:UDP704 2.1 64.3 1.0
OD2 D:ASP217 2.1 63.9 1.0
OD1 D:ASP217 2.2 60.6 1.0
O2A D:UDP704 2.2 60.1 1.0
CG D:ASP217 2.5 61.9 1.0
H5'1 D:UDP704 3.0 69.2 1.0
O3A D:UDP704 3.2 61.2 1.0
PB D:UDP704 3.2 63.8 1.0
PA D:UDP704 3.2 58.7 1.0
OD1 D:ASP218 3.7 63.3 1.0
HH12 D:ARG247 3.8 85.1 1.0
OD1 D:ASN317 3.8 71.5 1.0
H3' D:UDP704 3.8 64.7 1.0
HE D:ARG320 3.9 74.6 1.0
OD2 D:ASP218 3.9 61.3 1.0
HH21 D:ARG320 4.0 71.5 1.0
O1B D:UDP704 4.0 63.8 1.0
C5' D:UDP704 4.0 57.7 1.0
CB D:ASP217 4.0 59.6 1.0
O5' D:UDP704 4.1 58.1 1.0
HB3 D:ASP215 4.2 70.0 1.0
CG D:ASP218 4.2 61.2 1.0
HB2 D:ASP215 4.2 70.0 1.0
HB3 D:ASP217 4.3 71.5 1.0
OD2 D:ASP215 4.3 59.9 1.0
O D:THR318 4.4 72.3 1.0
O2B D:UDP704 4.4 66.5 1.0
HB2 D:ASP217 4.4 71.5 1.0
O1A D:UDP704 4.5 63.0 1.0
HB2 D:SER323 4.5 83.7 1.0
NH1 D:ARG247 4.5 71.0 1.0
CB D:ASP215 4.6 58.3 1.0
H5'2 D:UDP704 4.6 69.2 1.0
H D:ASP217 4.7 66.8 1.0
NE D:ARG320 4.7 62.2 1.0
NH2 D:ARG320 4.8 59.6 1.0
HH22 D:ARG247 4.8 82.3 1.0
C3' D:UDP704 4.8 54.0 1.0
HH11 D:ARG247 4.8 85.1 1.0
H D:THR318 4.9 83.8 1.0
CG D:ASP215 4.9 58.8 1.0
HB D:THR318 4.9 81.6 1.0
C4' D:UDP704 5.0 55.1 1.0
CG D:ASN317 5.0 72.2 1.0

Reference:

E.Stancanelli, J.A.Krahn, E.Viverette, R.Dutcher, V.Pagadala, M.J.Borgnia, J.Liu, L.C.Pedersen. Structural and Functional Analysis of Heparosan Synthase 2 From Pasteurella Multocida to Improve the Synthesis of Heparin Acs Catalysis V. 14 6577 2024.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.4C00677
Page generated: Sun Oct 6 14:04:21 2024

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