Atomistry » Manganese » PDB 2ypq-3au8 » 2zxq
Atomistry »
  Manganese »
    PDB 2ypq-3au8 »
      2zxq »

Manganese in PDB 2zxq: Crystal Structure of Endo-Alpha-N-Acetylgalactosaminidase From Bifidobacterium Longum (Engbf)

Enzymatic activity of Crystal Structure of Endo-Alpha-N-Acetylgalactosaminidase From Bifidobacterium Longum (Engbf)

All present enzymatic activity of Crystal Structure of Endo-Alpha-N-Acetylgalactosaminidase From Bifidobacterium Longum (Engbf):
3.2.1.97;

Protein crystallography data

The structure of Crystal Structure of Endo-Alpha-N-Acetylgalactosaminidase From Bifidobacterium Longum (Engbf), PDB code: 2zxq was solved by R.Suzuki, T.Katayama, H.Ashida, K.Yamamoto, M.Kitaoka, S.Fushinobu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.49 / 2.00
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 192.267, 192.267, 123.017, 90.00, 90.00, 120.00
R / Rfree (%) 17.2 / 19.6

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Endo-Alpha-N-Acetylgalactosaminidase From Bifidobacterium Longum (Engbf) (pdb code 2zxq). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of Endo-Alpha-N-Acetylgalactosaminidase From Bifidobacterium Longum (Engbf), PDB code: 2zxq:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 2zxq

Go back to Manganese Binding Sites List in 2zxq
Manganese binding site 1 out of 4 in the Crystal Structure of Endo-Alpha-N-Acetylgalactosaminidase From Bifidobacterium Longum (Engbf)


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 Endo-Alpha-N-Acetylgalactosaminidase From Bifidobacterium Longum (Engbf) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1

b:30.6
occ:1.00
OD1 A:ASP601 2.3 24.8 1.0
O A:ALA607 2.4 26.4 1.0
OD2 A:ASP612 2.4 21.8 1.0
OD1 A:ASN603 2.4 24.2 1.0
OD1 A:ASP612 2.4 21.6 1.0
O A:HOH78 2.5 24.3 1.0
OD1 A:ASP605 2.5 25.1 1.0
CG A:ASP612 2.7 21.2 1.0
CG A:ASP605 3.4 27.0 1.0
CG A:ASN603 3.4 26.3 1.0
CG A:ASP601 3.5 27.2 1.0
C A:ALA607 3.5 27.1 1.0
OD2 A:ASP605 3.8 25.8 1.0
ND2 A:ASN603 3.9 23.9 1.0
N A:ASP605 4.2 29.1 1.0
CA A:ASP601 4.2 25.3 1.0
CB A:ASP612 4.3 21.1 1.0
N A:ALA607 4.3 27.7 1.0
OD2 A:ASP601 4.3 26.3 1.0
N A:ASN603 4.3 26.0 1.0
CB A:ASP601 4.3 25.1 1.0
CA A:VAL608 4.4 25.8 1.0
N A:VAL608 4.4 25.6 1.0
CA A:ALA607 4.5 27.1 1.0
CB A:ASP605 4.5 27.4 1.0
C A:ASP601 4.5 25.4 1.0
OD1 A:ASN609 4.5 24.1 1.0
N A:GLU604 4.6 28.6 1.0
N A:GLU602 4.6 25.4 1.0
CB A:ASN603 4.7 25.9 1.0
CA A:ASP605 4.7 28.3 1.0
C A:ASN603 4.8 27.8 1.0
CA A:ASN603 4.8 26.6 1.0
N A:ASN609 4.8 23.0 1.0
N A:GLY606 4.8 28.6 1.0
CB A:ALA607 4.9 26.8 1.0
C A:ASP605 5.0 28.5 1.0
N A:ASP612 5.0 21.1 1.0

Manganese binding site 2 out of 4 in 2zxq

Go back to Manganese Binding Sites List in 2zxq
Manganese binding site 2 out of 4 in the Crystal Structure of Endo-Alpha-N-Acetylgalactosaminidase From Bifidobacterium Longum (Engbf)


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 Endo-Alpha-N-Acetylgalactosaminidase From Bifidobacterium Longum (Engbf) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn2

b:42.4
occ:1.00
OE1 A:GLU727 2.1 27.4 1.0
OD2 A:ASP752 2.2 24.8 1.0
O A:HOH1708 2.2 23.6 1.0
NE2 A:HIS1299 2.3 22.3 1.0
O A:HOH223 2.3 20.6 1.0
O A:HOH272 2.3 23.0 1.0
CD A:GLU727 3.1 27.2 1.0
CG A:ASP752 3.1 27.2 1.0
CD2 A:HIS1299 3.2 24.3 1.0
CE1 A:HIS1299 3.3 23.0 1.0
OE2 A:GLU727 3.4 25.0 1.0
OD1 A:ASP752 3.5 26.8 1.0
O A:HOH128 4.1 22.5 1.0
O A:HOH298 4.2 25.8 1.0
O A:HOH276 4.2 23.6 1.0
CA A:SER1301 4.3 25.6 1.0
O A:LEU1300 4.3 25.0 1.0
ND1 A:HIS1299 4.4 24.0 1.0
CG A:HIS1299 4.4 23.4 1.0
CB A:ASP752 4.4 25.2 1.0
CG A:GLU727 4.4 25.6 1.0
O A:HOH248 4.4 23.0 1.0
CB A:GLU727 4.7 24.8 1.0
N A:GLU1302 4.8 25.9 1.0
OG A:SER683 4.8 20.9 1.0
CB A:LEU751 4.9 24.7 1.0
CB A:SER1301 4.9 25.6 1.0

Manganese binding site 3 out of 4 in 2zxq

Go back to Manganese Binding Sites List in 2zxq
Manganese binding site 3 out of 4 in the Crystal Structure of Endo-Alpha-N-Acetylgalactosaminidase From Bifidobacterium Longum (Engbf)


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 Endo-Alpha-N-Acetylgalactosaminidase From Bifidobacterium Longum (Engbf) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn3

b:33.2
occ:1.00
ND2 A:ASN1135 2.3 20.5 1.0
O A:ALA1136 2.4 25.5 1.0
O A:GLY1108 2.4 26.1 1.0
OD2 A:ASP1248 2.4 24.8 1.0
O A:HOH1724 2.4 25.9 1.0
O A:HOH167 2.5 18.5 1.0
OD1 A:ASP1248 2.7 23.4 1.0
CG A:ASP1248 2.9 27.2 1.0
C A:GLY1108 3.4 24.8 1.0
C A:ALA1136 3.5 26.4 1.0
CG A:ASN1135 3.6 25.0 1.0
CA A:GLY1108 3.8 24.5 1.0
N A:ALA1136 3.9 25.0 1.0
C A:ASN1135 4.1 25.3 1.0
CA A:ALA1136 4.3 25.9 1.0
OD1 A:ASN1135 4.3 28.2 1.0
CB A:ASP1248 4.4 26.0 1.0
OD1 A:ASP1249 4.4 23.1 1.0
O A:ASN1135 4.5 24.9 1.0
NE2 A:HIS1203 4.5 24.9 1.0
N A:PHE1109 4.6 25.3 1.0
ND2 A:ASN1110 4.6 21.2 1.0
N A:MET1137 4.6 27.1 1.0
O A:HOH122 4.6 22.0 1.0
CA A:ASN1135 4.7 24.6 1.0
O A:HOH297 4.7 24.2 1.0
CB A:ASN1135 4.7 23.4 1.0
CA A:MET1137 4.8 27.5 1.0
CB A:ALA1136 4.9 25.6 1.0
OD1 A:ASN1110 4.9 25.8 1.0
CB A:PHE1109 4.9 25.2 1.0
CG A:ASP1249 5.0 27.3 1.0
OD2 A:ASP1249 5.0 29.8 1.0

Manganese binding site 4 out of 4 in 2zxq

Go back to Manganese Binding Sites List in 2zxq
Manganese binding site 4 out of 4 in the Crystal Structure of Endo-Alpha-N-Acetylgalactosaminidase From Bifidobacterium Longum (Engbf)


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 Endo-Alpha-N-Acetylgalactosaminidase From Bifidobacterium Longum (Engbf) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn4

b:37.6
occ:1.00
O A:GLY1274 2.3 28.1 1.0
OE2 A:GLU1276 2.3 32.2 1.0
O A:ASP1322 2.3 32.4 1.0
O A:TRP1325 2.4 27.8 1.0
O A:HOH1930 2.4 30.8 1.0
OD2 A:ASP1442 2.5 28.2 1.0
OD1 A:ASP1442 2.6 28.4 1.0
CG A:ASP1442 2.9 28.3 1.0
C A:GLY1274 3.4 27.9 1.0
C A:ASP1322 3.5 32.6 1.0
CD A:GLU1276 3.5 31.3 1.0
C A:TRP1325 3.6 28.1 1.0
CA A:GLY1274 3.9 28.2 1.0
CG A:GLU1276 4.0 29.7 1.0
N A:TRP1325 4.2 27.9 1.0
CB A:ASP1322 4.2 35.6 1.0
CA A:ASP1322 4.3 34.4 1.0
CA A:TRP1325 4.4 28.0 1.0
OG A:SER1326 4.4 28.2 1.0
N A:GLY1323 4.4 31.2 1.0
CB A:ASP1442 4.4 30.6 1.0
O A:HOH2258 4.5 41.5 1.0
N A:ASP1322 4.5 33.4 1.0
OE1 A:GLU1276 4.5 30.2 1.0
CA A:GLY1323 4.5 30.3 1.0
N A:PHE1275 4.5 28.9 1.0
N A:SER1326 4.5 27.3 1.0
OD1 A:ASN1443 4.7 38.2 1.0
CA A:SER1326 4.7 26.9 1.0
N A:THR1324 4.8 29.8 1.0
CB A:TRP1325 4.8 28.2 1.0
CB A:PHE1275 4.8 28.8 1.0
C A:GLY1323 4.8 29.4 1.0
CA A:PHE1275 5.0 29.4 1.0
C A:PHE1275 5.0 30.0 1.0
N A:GLU1276 5.0 29.6 1.0

Reference:

R.Suzuki, T.Katayama, M.Kitaoka, H.Kumagai, T.Wakagi, H.Shoun, H.Ashida, K.Yamamoto, S.Fushinobu. Crystallographic and Mutational Analyses of Substrate Recognition of Endo-{Alpha}-N-Acetylgalactosaminidase From Bifidobacterium Longum. J.Biochem. 2009.
ISSN: ISSN 0021-924X
PubMed: 19502354
DOI: 10.1093/JB/MVP086
Page generated: Sat Oct 5 15:38:01 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy