Zinc in PDB 6obd: Crystal Structure of Anti-GLD52 Fab Complex with Human GLD52 Peptide Mimetic
Protein crystallography data
The structure of Crystal Structure of Anti-GLD52 Fab Complex with Human GLD52 Peptide Mimetic, PDB code: 6obd
was solved by
R.Wei,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.53 /
2.20
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
54.400,
131.200,
133.800,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
23.4 /
30.7
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Anti-GLD52 Fab Complex with Human GLD52 Peptide Mimetic
(pdb code 6obd). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the
Crystal Structure of Anti-GLD52 Fab Complex with Human GLD52 Peptide Mimetic, PDB code: 6obd:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
Zinc binding site 1 out
of 5 in 6obd
Go back to
Zinc Binding Sites List in 6obd
Zinc binding site 1 out
of 5 in the Crystal Structure of Anti-GLD52 Fab Complex with Human GLD52 Peptide Mimetic
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structure of Anti-GLD52 Fab Complex with Human GLD52 Peptide Mimetic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:30.0
occ:1.00
|
OE2
|
A:GLU86
|
1.4
|
27.3
|
1.0
|
OE2
|
L:GLU84
|
1.7
|
33.0
|
1.0
|
OE2
|
A:GLU84
|
1.7
|
29.3
|
1.0
|
OE2
|
L:GLU86
|
1.8
|
32.4
|
1.0
|
CD
|
A:GLU86
|
2.5
|
29.7
|
1.0
|
CD
|
L:GLU86
|
2.6
|
32.2
|
1.0
|
CD
|
L:GLU84
|
2.9
|
30.0
|
1.0
|
CD
|
A:GLU84
|
2.9
|
26.5
|
1.0
|
OE1
|
L:GLU86
|
3.0
|
30.5
|
1.0
|
OE1
|
A:GLU86
|
3.1
|
28.5
|
1.0
|
OE1
|
A:GLU84
|
3.6
|
29.0
|
1.0
|
CB
|
L:GLU84
|
3.7
|
25.7
|
1.0
|
CG
|
L:GLU84
|
3.7
|
29.4
|
1.0
|
OE1
|
L:GLU84
|
3.8
|
33.2
|
1.0
|
CG
|
A:GLU86
|
3.8
|
26.9
|
1.0
|
NH1
|
L:ARG66
|
3.8
|
23.0
|
1.0
|
CG
|
L:GLU86
|
3.9
|
29.7
|
1.0
|
CG
|
A:GLU84
|
4.0
|
26.0
|
1.0
|
CB
|
A:GLU84
|
4.0
|
25.8
|
1.0
|
NH1
|
A:ARG66
|
4.0
|
26.3
|
1.0
|
CZ
|
L:ARG66
|
4.7
|
27.8
|
1.0
|
CZ
|
A:ARG66
|
4.9
|
28.2
|
1.0
|
|
Zinc binding site 2 out
of 5 in 6obd
Go back to
Zinc Binding Sites List in 6obd
Zinc binding site 2 out
of 5 in the Crystal Structure of Anti-GLD52 Fab Complex with Human GLD52 Peptide Mimetic
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structure of Anti-GLD52 Fab Complex with Human GLD52 Peptide Mimetic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn301
b:30.0
occ:0.50
|
O3
|
E:OPE101
|
2.1
|
51.1
|
1.0
|
P
|
E:OPE101
|
3.6
|
51.7
|
1.0
|
O2
|
E:OPE101
|
4.2
|
50.7
|
1.0
|
O4
|
E:OPE101
|
4.3
|
49.6
|
1.0
|
O1
|
E:OPE101
|
4.6
|
49.3
|
1.0
|
|
Zinc binding site 3 out
of 5 in 6obd
Go back to
Zinc Binding Sites List in 6obd
Zinc binding site 3 out
of 5 in the Crystal Structure of Anti-GLD52 Fab Complex with Human GLD52 Peptide Mimetic
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structure of Anti-GLD52 Fab Complex with Human GLD52 Peptide Mimetic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
L:Zn301
b:30.0
occ:1.00
|
OE2
|
B:GLU1
|
1.1
|
33.8
|
1.0
|
OD1
|
L:ASN142
|
1.7
|
35.1
|
1.0
|
CE1
|
H:HIS165
|
1.9
|
20.0
|
1.0
|
ND2
|
L:ASN141
|
2.3
|
21.0
|
1.0
|
CD
|
B:GLU1
|
2.4
|
33.4
|
1.0
|
CG
|
L:ASN142
|
2.9
|
32.3
|
1.0
|
ND1
|
H:HIS165
|
2.9
|
19.8
|
1.0
|
NE2
|
H:HIS165
|
2.9
|
25.3
|
1.0
|
OE1
|
B:GLU1
|
3.2
|
33.2
|
1.0
|
CG
|
L:ASN141
|
3.2
|
25.9
|
1.0
|
OD1
|
L:ASN141
|
3.4
|
25.5
|
1.0
|
ND2
|
L:ASN142
|
3.5
|
34.7
|
1.0
|
CG
|
B:GLU1
|
3.5
|
33.6
|
1.0
|
OG
|
L:SER178
|
3.9
|
24.7
|
1.0
|
CD2
|
H:HIS165
|
4.1
|
23.8
|
1.0
|
CG
|
H:HIS165
|
4.1
|
24.6
|
1.0
|
O
|
H:GLY163
|
4.1
|
24.8
|
1.0
|
CB
|
L:ASN142
|
4.1
|
27.0
|
1.0
|
OG1
|
H:THR184
|
4.5
|
28.6
|
1.0
|
CB
|
L:ASN141
|
4.6
|
24.2
|
1.0
|
C
|
H:GLY163
|
4.7
|
25.4
|
1.0
|
CA
|
H:GLY163
|
4.7
|
26.0
|
1.0
|
N
|
L:ASN142
|
4.8
|
25.9
|
1.0
|
O
|
L:HOH478
|
4.8
|
30.4
|
1.0
|
CB
|
B:GLU1
|
4.9
|
31.4
|
1.0
|
CA
|
L:ASN142
|
5.0
|
25.9
|
1.0
|
|
Zinc binding site 4 out
of 5 in 6obd
Go back to
Zinc Binding Sites List in 6obd
Zinc binding site 4 out
of 5 in the Crystal Structure of Anti-GLD52 Fab Complex with Human GLD52 Peptide Mimetic
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Crystal Structure of Anti-GLD52 Fab Complex with Human GLD52 Peptide Mimetic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Zn301
b:30.0
occ:1.00
|
OE1
|
H:GLU1
|
1.5
|
40.0
|
1.0
|
NE2
|
B:HIS165
|
2.0
|
21.5
|
1.0
|
ND2
|
A:ASN141
|
2.3
|
17.4
|
1.0
|
ND2
|
A:ASN142
|
2.6
|
30.4
|
1.0
|
CD
|
H:GLU1
|
2.7
|
36.0
|
1.0
|
CD2
|
B:HIS165
|
2.9
|
23.0
|
1.0
|
CE1
|
B:HIS165
|
3.0
|
20.9
|
1.0
|
OD1
|
A:ASN142
|
3.0
|
40.0
|
1.0
|
CG
|
A:ASN142
|
3.2
|
33.8
|
1.0
|
CG
|
A:ASN141
|
3.2
|
23.4
|
1.0
|
OE2
|
H:GLU1
|
3.4
|
38.4
|
1.0
|
OD1
|
A:ASN141
|
3.5
|
23.1
|
1.0
|
CG
|
H:GLU1
|
3.9
|
36.4
|
1.0
|
OG
|
A:SER178
|
4.0
|
22.0
|
1.0
|
ND1
|
B:HIS165
|
4.0
|
17.8
|
1.0
|
CG
|
B:HIS165
|
4.1
|
22.9
|
1.0
|
O
|
B:GLY163
|
4.4
|
23.5
|
1.0
|
O
|
A:HOH478
|
4.4
|
19.5
|
1.0
|
CG2
|
B:THR184
|
4.5
|
24.1
|
1.0
|
CB
|
A:ASN142
|
4.6
|
27.3
|
1.0
|
CB
|
A:ASN141
|
4.7
|
24.2
|
1.0
|
N
|
A:ASN142
|
4.7
|
24.8
|
1.0
|
C
|
B:GLY163
|
4.8
|
23.6
|
1.0
|
CA
|
B:GLY163
|
4.8
|
24.3
|
1.0
|
CB
|
B:THR184
|
4.9
|
26.1
|
1.0
|
CB
|
H:GLU1
|
4.9
|
33.5
|
1.0
|
|
Zinc binding site 5 out
of 5 in 6obd
Go back to
Zinc Binding Sites List in 6obd
Zinc binding site 5 out
of 5 in the Crystal Structure of Anti-GLD52 Fab Complex with Human GLD52 Peptide Mimetic
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Crystal Structure of Anti-GLD52 Fab Complex with Human GLD52 Peptide Mimetic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn102
b:30.0
occ:0.50
|
O1
|
E:OPE101
|
1.9
|
49.3
|
1.0
|
P
|
E:OPE101
|
3.3
|
51.7
|
1.0
|
O2
|
E:OPE101
|
3.7
|
50.7
|
1.0
|
O4
|
E:OPE101
|
4.3
|
49.6
|
1.0
|
O3
|
E:OPE101
|
4.4
|
51.1
|
1.0
|
CA
|
E:OPE101
|
4.4
|
49.8
|
1.0
|
O
|
E:SER12
|
4.9
|
25.2
|
1.0
|
|
Reference:
H.Qiu,
R.Wei,
J.Jaworski,
E.Boudanova,
H.Hughes,
S.Vanpatten,
A.Lund,
J.Day,
Y.Zhou,
T.Mcsherry,
C.Q.Pan,
R.Sendak.
Engineering An Anti-CD52 Antibody For Enhanced Deamidation Stability. Mabs V. 11 1266 2019.
ISSN: ESSN 1942-0870
PubMed: 31199181
DOI: 10.1080/19420862.2019.1631117
Page generated: Tue Oct 29 04:12:31 2024
|