- SASDDQ8: The complex formed between the class II apurinic/apyrimidinic-end... -
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ID or keywords:
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Basic information
Entry
Database: SASBDB / ID: SASDDQ8
Sample
The complex formed between the class II apurinic/apyrimidinic-endonuclease/3'-5' exonuclease III (XthA) bound to the BRCT domain from Mycobacterium tuberculosis DNA ligase
Probable exodeoxyribonuclease III protein XthA (protein), MtbXthA, Mycobacterium tuberculosis
M. tb. LigA BRCT domain (protein), BRCT domain, Mycobacterium tuberculosis
Function / homology
Function and homology information
: / DNA ligase (NAD+) / DNA ligase (NAD+) activity / base-excision repair, DNA ligation / exodeoxyribonuclease III / DNA ligation / peptidoglycan-based cell wall / endonuclease activity / DNA replication / DNA repair ...: / DNA ligase (NAD+) / DNA ligase (NAD+) activity / base-excision repair, DNA ligation / exodeoxyribonuclease III / DNA ligation / peptidoglycan-based cell wall / endonuclease activity / DNA replication / DNA repair / magnesium ion binding / DNA binding / plasma membrane / cytosol Similarity search - Function
Exodeoxyribonuclease III-like / Zinc-finger, NAD-dependent DNA ligase C4-type / NAD-dependent DNA ligase C4 zinc finger domain / NAD-dependent DNA ligase, active site / NAD-dependent DNA ligase, conserved site / NAD-dependent DNA ligase signature 1. / NAD-dependent DNA ligase signature 2. / NAD-dependent DNA ligase / NAD-dependent DNA ligase, OB-fold / NAD-dependent DNA ligase, adenylation ...Exodeoxyribonuclease III-like / Zinc-finger, NAD-dependent DNA ligase C4-type / NAD-dependent DNA ligase C4 zinc finger domain / NAD-dependent DNA ligase, active site / NAD-dependent DNA ligase, conserved site / NAD-dependent DNA ligase signature 1. / NAD-dependent DNA ligase signature 2. / NAD-dependent DNA ligase / NAD-dependent DNA ligase, OB-fold / NAD-dependent DNA ligase, adenylation / NAD-dependent DNA ligase, N-terminal / NAD-dependent DNA ligase adenylation domain / NAD-dependent DNA ligase OB-fold domain / Ligase N family / DisA/LigA, helix-hairpin-helix motif / Helix-hairpin-helix motif / AP endonuclease 1, binding site / AP endonucleases family 1 signature 1. / AP endonuclease 1 / AP endonucleases family 1 profile. / RuvA domain 2-like / Endonuclease/exonuclease/phosphatase / Endonuclease/Exonuclease/phosphatase family / Endonuclease/exonuclease/phosphatase superfamily / BRCA1 C Terminus (BRCT) domain / breast cancer carboxy-terminal domain / BRCT domain profile. / BRCT domain / BRCT domain superfamily / Nucleic acid-binding, OB-fold Similarity search - Domain/homology
Name: The complex formed between the class II apurinic/apyrimidinic-endonuclease/3'-5' exonuclease III (XthA) bound to the BRCT domain from Mycobacterium tuberculosis DNA ligase Specimen concentration: 4.6 mg/ml / Entity id: 1121 / 1122
Buffer
Name: 50 mM Tris-HCl 500 mM NaCl 5mM β-mercaptoethanol / pH: 8
Entity #1121
Name: MtbXthA / Type: protein / Description: Probable exodeoxyribonuclease III protein XthA / Formula weight: 32.931 / Num. of mol.: 1 / Source: Mycobacterium tuberculosis / References: UniProt: A0A0T9L251 Sequence: MPDGTIDGGH PQRPASPRLR SPLLRLATWN VNSIRTRLDR VLDWLGRADV DVLAMQETKC PDGQFPALPL FELGYDVAHV GFDQWNGVAI ASRVGLDDVR VGFDGQPSWS GKPEVAATTE ARALGATCGG IRVWSLYVPN GRALDDPHYT YKLDWLAALR DTAEGWLRDD ...Sequence:
Title: The complex formed between the class II apurinic/apyrimidinic-endonuclease/3'-5' exonuclease III (XthA) bound to the BRCT domain from Mycobacterium tuberculosis DNA ligase Measurement date: Mar 9, 2018 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 1 sec. / Number of frames: 10 / Unit: 1/nm /
Min
Max
Q
0.0309
4.9277
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 290 /
Min
Max
Q
0.0637909
1.42193
P(R) point
1
290
R
0
18.48
Result
Type of curve: single_conc Comments: The ab initio model displayed in this entry represents the spatially aligned, volume and bead-occupancy-corrected (averaged) representation of the protein (DAMFILT). The displayed fit ...Comments: The ab initio model displayed in this entry represents the spatially aligned, volume and bead-occupancy-corrected (averaged) representation of the protein (DAMFILT). The displayed fit corresponds to an individual model fit to the SAXS data.
Experimental
Porod
MW
45.68 kDa
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Volume
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112 nm3
P(R)
P(R) error
Guinier
Guinier error
Forward scattering, I0
100.6
0.2
98.53
0.1
Radius of gyration, Rg
4.06 nm
0.03
3.69 nm
0.01
Min
Max
D
-
18.48
Guinier point
8
69
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