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
|