Zinc in PDB 3pih: T. Maritima Uvra in Complex with Fluorescein-Modified Dna
Protein crystallography data
The structure of T. Maritima Uvra in Complex with Fluorescein-Modified Dna, PDB code: 3pih
was solved by
M.Jaciuk,
E.Nowak,
M.Nowotny,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
48.08 /
2.90
|
Space group
|
P 42
|
Cell size a, b, c (Å), α, β, γ (°)
|
107.510,
107.510,
108.256,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.8 /
26.5
|
Zinc Binding Sites:
The binding sites of Zinc atom in the T. Maritima Uvra in Complex with Fluorescein-Modified Dna
(pdb code 3pih). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
T. Maritima Uvra in Complex with Fluorescein-Modified Dna, PDB code: 3pih:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 3pih
Go back to
Zinc Binding Sites List in 3pih
Zinc binding site 1 out
of 3 in the T. Maritima Uvra in Complex with Fluorescein-Modified Dna
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of T. Maritima Uvra in Complex with Fluorescein-Modified Dna within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn917
b:68.4
occ:1.00
|
SG
|
A:CYS719
|
2.2
|
74.3
|
1.0
|
SG
|
A:CYS716
|
2.4
|
78.4
|
1.0
|
SG
|
A:CYS742
|
2.4
|
65.8
|
1.0
|
SG
|
A:CYS739
|
2.5
|
80.6
|
1.0
|
CB
|
A:CYS716
|
2.9
|
70.8
|
1.0
|
CB
|
A:CYS742
|
3.1
|
65.7
|
1.0
|
CB
|
A:CYS739
|
3.2
|
64.2
|
1.0
|
CB
|
A:CYS719
|
3.4
|
73.1
|
1.0
|
N
|
A:CYS719
|
3.7
|
77.7
|
1.0
|
N
|
A:CYS742
|
3.8
|
71.6
|
1.0
|
CA
|
A:CYS742
|
4.1
|
73.5
|
1.0
|
CA
|
A:CYS719
|
4.2
|
71.3
|
1.0
|
CA
|
A:CYS716
|
4.2
|
67.2
|
1.0
|
CB
|
A:ALA718
|
4.2
|
64.0
|
1.0
|
O
|
A:CYS716
|
4.2
|
70.7
|
1.0
|
C
|
A:CYS716
|
4.4
|
71.8
|
1.0
|
CA
|
A:ARG746
|
4.5
|
66.7
|
1.0
|
CB
|
A:VAL741
|
4.5
|
63.0
|
1.0
|
CA
|
A:CYS739
|
4.6
|
77.4
|
1.0
|
CA
|
A:GLY723
|
4.7
|
64.1
|
1.0
|
C
|
A:ALA718
|
4.7
|
75.4
|
1.0
|
N
|
A:GLY723
|
4.8
|
56.6
|
1.0
|
N
|
A:ALA718
|
4.8
|
74.5
|
1.0
|
CA
|
A:ALA718
|
4.8
|
60.7
|
1.0
|
C
|
A:VAL741
|
4.9
|
69.6
|
1.0
|
N
|
A:ARG746
|
4.9
|
69.1
|
1.0
|
C
|
A:CYS719
|
4.9
|
71.3
|
1.0
|
|
Zinc binding site 2 out
of 3 in 3pih
Go back to
Zinc Binding Sites List in 3pih
Zinc binding site 2 out
of 3 in the T. Maritima Uvra in Complex with Fluorescein-Modified Dna
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of T. Maritima Uvra in Complex with Fluorescein-Modified Dna within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn918
b:70.4
occ:1.00
|
SG
|
A:CYS384
|
2.4
|
67.0
|
1.0
|
SG
|
A:CYS387
|
2.5
|
61.7
|
1.0
|
SG
|
A:CYS279
|
2.6
|
61.3
|
1.0
|
SG
|
A:CYS276
|
2.6
|
70.6
|
1.0
|
CB
|
A:CYS279
|
3.0
|
66.2
|
1.0
|
CB
|
A:CYS276
|
3.1
|
64.0
|
1.0
|
CB
|
A:CYS387
|
3.1
|
56.6
|
1.0
|
CB
|
A:CYS384
|
3.2
|
77.6
|
1.0
|
N
|
A:CYS387
|
3.7
|
66.7
|
1.0
|
CA
|
A:CYS387
|
4.0
|
55.4
|
1.0
|
N
|
A:CYS279
|
4.1
|
70.2
|
1.0
|
CA
|
A:CYS279
|
4.1
|
66.2
|
1.0
|
OD1
|
A:ASN278
|
4.1
|
76.2
|
1.0
|
CA
|
A:CYS276
|
4.5
|
60.5
|
1.0
|
C
|
A:ASN278
|
4.6
|
76.1
|
1.0
|
CA
|
A:CYS384
|
4.6
|
75.6
|
1.0
|
CB
|
A:VAL386
|
4.8
|
67.6
|
1.0
|
C
|
A:CYS276
|
4.8
|
67.3
|
1.0
|
C
|
A:CYS279
|
4.9
|
70.3
|
1.0
|
C
|
A:VAL386
|
4.9
|
70.4
|
1.0
|
O
|
A:ASN278
|
4.9
|
82.8
|
1.0
|
O
|
A:CYS276
|
4.9
|
66.6
|
1.0
|
C
|
A:CYS387
|
4.9
|
57.2
|
1.0
|
CG
|
A:ASN278
|
4.9
|
65.1
|
1.0
|
O
|
A:ARG391
|
5.0
|
56.6
|
1.0
|
|
Zinc binding site 3 out
of 3 in 3pih
Go back to
Zinc Binding Sites List in 3pih
Zinc binding site 3 out
of 3 in the T. Maritima Uvra in Complex with Fluorescein-Modified Dna
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of T. Maritima Uvra in Complex with Fluorescein-Modified Dna within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn919
b:80.2
occ:0.70
|
SG
|
A:CYS123
|
2.3
|
81.8
|
1.0
|
SG
|
A:CYS255
|
2.4
|
0.5
|
1.0
|
SG
|
A:CYS120
|
2.6
|
96.1
|
1.0
|
CB
|
A:CYS123
|
2.8
|
89.9
|
1.0
|
SG
|
A:CYS252
|
2.9
|
77.5
|
1.0
|
CB
|
A:CYS120
|
3.5
|
94.8
|
1.0
|
CB
|
A:CYS255
|
3.7
|
1.0
|
1.0
|
N
|
A:CYS123
|
3.9
|
0.3
|
1.0
|
CG
|
A:GLU122
|
3.9
|
0.4
|
1.0
|
CA
|
A:CYS123
|
3.9
|
97.2
|
1.0
|
CB
|
A:CYS252
|
4.0
|
86.7
|
1.0
|
OE1
|
A:GLU122
|
4.1
|
0.2
|
1.0
|
CB
|
A:VAL254
|
4.5
|
86.5
|
1.0
|
CD
|
A:GLU122
|
4.5
|
0.6
|
1.0
|
N
|
A:CYS255
|
4.6
|
96.8
|
1.0
|
C
|
A:VAL254
|
4.7
|
88.5
|
1.0
|
CA
|
A:CYS255
|
4.8
|
95.9
|
1.0
|
C
|
A:CYS123
|
4.8
|
99.9
|
1.0
|
CA
|
A:CYS120
|
5.0
|
88.4
|
1.0
|
|
Reference:
M.Jaciuk,
E.Nowak,
K.Skowronek,
A.Tanska,
M.Nowotny.
Structure of Uvra Nucleotide Excision Repair Protein in Complex with Modified Dna. Nat.Struct.Mol.Biol. V. 18 191 2011.
ISSN: ISSN 1545-9993
PubMed: 21240268
DOI: 10.1038/NSMB.1973
Page generated: Sat Oct 26 11:27:03 2024
|