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- PDB-3k0h: The crystal structure of BRCA1 BRCT in complex with a minimal rec... -

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Basic information

Entry
Database: PDB / ID: 3k0h
TitleThe crystal structure of BRCA1 BRCT in complex with a minimal recognition tetrapeptide with an amidated C-terminus
Components
  • Breast cancer type 1 susceptibility protein
  • phospho peptide
KeywordsPROTEIN BINDING / BRCA1 / BRCT domain / DNA damage response / phospho peptide interactions / BACH1 / Alternative initiation / Cell cycle / Disease mutation / DNA damage / DNA repair / DNA-binding / Fatty acid biosynthesis / Ligase / Lipid synthesis / Metal-binding / Nucleus / Phosphoprotein / Tumor suppressor / Ubl conjugation pathway / Zinc-finger
Function / homology
Function and homology information


Defective DNA double strand break response due to BRCA1 loss of function / Defective DNA double strand break response due to BARD1 loss of function / : / BRCA1-BARD1 complex / BRCA1-C complex / BRCA1-B complex / BRCA1-A complex / random inactivation of X chromosome / negative regulation of centriole replication / negative regulation of intracellular estrogen receptor signaling pathway ...Defective DNA double strand break response due to BRCA1 loss of function / Defective DNA double strand break response due to BARD1 loss of function / : / BRCA1-BARD1 complex / BRCA1-C complex / BRCA1-B complex / BRCA1-A complex / random inactivation of X chromosome / negative regulation of centriole replication / negative regulation of intracellular estrogen receptor signaling pathway / gamma-tubulin ring complex / nuclear ubiquitin ligase complex / DNA strand resection involved in replication fork processing / chordate embryonic development / negative regulation of fatty acid biosynthetic process / cellular response to indole-3-methanol / homologous recombination / lateral element / XY body / protein K6-linked ubiquitination / regulation of DNA damage checkpoint / dosage compensation by inactivation of X chromosome / negative regulation of gene expression via chromosomal CpG island methylation / Impaired BRCA2 binding to PALB2 / : / mitotic G2/M transition checkpoint / postreplication repair / DNA repair complex / RNA polymerase binding / centrosome cycle / Defective homologous recombination repair (HRR) due to BRCA1 loss of function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function / Homologous DNA Pairing and Strand Exchange / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / Resolution of D-loop Structures through Holliday Junction Intermediates / HDR through Single Strand Annealing (SSA) / Impaired BRCA2 binding to RAD51 / intracellular non-membrane-bounded organelle / response to ionizing radiation / DNA-binding transcription activator activity / Transcriptional Regulation by E2F6 / mitotic G2 DNA damage checkpoint signaling / Presynaptic phase of homologous DNA pairing and strand exchange / negative regulation of cell cycle / positive regulation of vascular endothelial growth factor production / negative regulation of reactive oxygen species metabolic process / localization / regulation of DNA repair / protein autoubiquitination / SUMOylation of DNA damage response and repair proteins / ubiquitin ligase complex / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / positive regulation of DNA repair / Meiotic synapsis / tubulin binding / male germ cell nucleus / chromosome segregation / cellular response to ionizing radiation / TP53 Regulates Transcription of DNA Repair Genes / Nonhomologous End-Joining (NHEJ) / double-strand break repair via homologous recombination / RING-type E3 ubiquitin transferase / HDR through Homologous Recombination (HRR) / G2/M DNA damage checkpoint / negative regulation of cell growth / Metalloprotease DUBs / Meiotic recombination / ubiquitin-protein transferase activity / fatty acid biosynthetic process / positive regulation of angiogenesis / double-strand break repair / intrinsic apoptotic signaling pathway in response to DNA damage / KEAP1-NFE2L2 pathway / p53 binding / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / chromosome / Neddylation / cellular response to tumor necrosis factor / Processing of DNA double-strand break ends / Regulation of TP53 Activity through Phosphorylation / damaged DNA binding / transcription coactivator activity / nuclear body / protein ubiquitination / transcription cis-regulatory region binding / regulation of cell cycle / ribonucleoprotein complex / DNA repair / negative regulation of DNA-templated transcription / DNA damage response / ubiquitin protein ligase binding / positive regulation of gene expression / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / enzyme binding / positive regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / RNA binding
Similarity search - Function
Breast cancer type 1 susceptibility protein (BRCA1) / BRCA1, serine-rich domain / BRCA1-associated / Serine-rich domain associated with BRCT / BRCT domain / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / BRCA1 C Terminus (BRCT) domain / breast cancer carboxy-terminal domain / Zinc finger, RING-type, conserved site ...Breast cancer type 1 susceptibility protein (BRCA1) / BRCA1, serine-rich domain / BRCA1-associated / Serine-rich domain associated with BRCT / BRCT domain / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / BRCA1 C Terminus (BRCT) domain / breast cancer carboxy-terminal domain / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / BRCT domain profile. / BRCT domain / BRCT domain superfamily / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / Zinc finger, RING/FYVE/PHD-type / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
NICKEL (II) ION / Breast cancer type 1 susceptibility protein
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.7 Å
AuthorsCampbell, S.J. / Edwards, R.A. / Glover, J.N.
CitationJournal: Structure / Year: 2010
Title: Comparison of the Structures and Peptide Binding Specificities of the BRCT Domains of MDC1 and BRCA1
Authors: Campbell, S.J. / Edwards, R.A. / Glover, J.N.
History
DepositionSep 24, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 2, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Nov 1, 2017Group: Refinement description / Category: software

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Breast cancer type 1 susceptibility protein
B: phospho peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,2854
Polymers25,1912
Non-polymers942
Water32418
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area950 Å2
ΔGint-23 kcal/mol
Surface area11090 Å2
MethodPISA
Unit cell
Length a, b, c (Å)115.075, 115.075, 123.255
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number178
Space group name H-MP6122

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Components

#1: Protein Breast cancer type 1 susceptibility protein / RING finger protein 53


Mass: 24662.434 Da / Num. of mol.: 1 / Fragment: BRCT Domain (UNP residues 1646 to 1859)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: BRCA1, RNF53 / Plasmid: pLM1-CD6 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 Gold / References: UniProt: P38398
#2: Protein/peptide phospho peptide


Mass: 528.472 Da / Num. of mol.: 1 / Source method: obtained synthetically
Details: This sequence occurs naturally in humans in the BACH1/BRIP1 protein. The peptide is chemically synthesized.
#3: Chemical ChemComp-NI / NICKEL (II) ION / Nickel


Mass: 58.693 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Ni
#4: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 18 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 4.69 Å3/Da / Density % sol: 73.76 %
Crystal growTemperature: 298 K / Method: vapor diffusion / pH: 7.3
Details: Tris-HCl, Li2SO4, NiCl2, pH 7.3, VAPOR DIFFUSION, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.97934 Å
DetectorType: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Jan 21, 2008
RadiationMonochromator: DCM / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97934 Å / Relative weight: 1
ReflectionResolution: 2.65→50 Å / Num. obs: 14444 / % possible obs: 99.1 % / Redundancy: 6.8 % / Rmerge(I) obs: 0.063 / Χ2: 0.942 / Net I/σ(I): 16.1
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2Diffraction-ID% possible all
2.65-2.745.60.51314140.672199.4
2.74-2.857.10.42614130.7241100
2.85-2.987.20.26814220.7891100
2.98-3.147.20.1614150.8931100
3.14-3.347.20.11614360.9841100
3.34-3.67.10.08214521.0841100
3.6-3.967.10.06614441.0911100
3.96-4.536.90.06114561.084199.8
4.53-5.716.70.05514921.0541100
5.71-506.10.0415000.976192.9

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Phasing

PhasingMethod: molecular replacement
Phasing MRRfactor: 47.88 / Model details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation2.6 Å29.18 Å
Translation2.6 Å29.18 Å

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHASER2.1.4phasing
REFMAC5.5.0066refinement
PDB_EXTRACT3.005data extraction
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.7→29.44 Å / Cor.coef. Fo:Fc: 0.927 / Cor.coef. Fo:Fc free: 0.895 / Occupancy max: 1 / Occupancy min: 0.5 / SU B: 27.192 / SU ML: 0.269 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.369 / ESU R Free: 0.299 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : RESIDUAL ONLY
RfactorNum. reflection% reflectionSelection details
Rfree0.296 682 5 %RANDOM
Rwork0.247 ---
obs0.25 13654 99.19 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso max: 82.95 Å2 / Biso mean: 49.86 Å2 / Biso min: 31.65 Å2
Baniso -1Baniso -2Baniso -3
1--0.07 Å2-0.03 Å20 Å2
2---0.07 Å20 Å2
3---0.1 Å2
Refinement stepCycle: LAST / Resolution: 2.7→29.44 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1731 0 2 18 1751
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0221773
X-RAY DIFFRACTIONr_angle_refined_deg1.1051.9422407
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.1365213
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.31123.85583
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.78615.049304
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.6341511
X-RAY DIFFRACTIONr_chiral_restr0.0740.2267
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.0211336
X-RAY DIFFRACTIONr_mcbond_it0.4061.51070
X-RAY DIFFRACTIONr_mcangle_it0.77221745
X-RAY DIFFRACTIONr_scbond_it1.0233703
X-RAY DIFFRACTIONr_scangle_it1.7184.5662
LS refinement shellResolution: 2.7→2.77 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.365 48 -
Rwork0.31 941 -
all-989 -
obs--99.9 %
Refinement TLS params.Method: refined / Origin x: -18.9297 Å / Origin y: 49.1367 Å / Origin z: -3.921 Å
111213212223313233
T0.0703 Å2-0.0026 Å20.0402 Å2-0.4869 Å20.081 Å2--0.0545 Å2
L16.6566 °23.7151 °2-2.0147 °2-3.0061 °2-1.0208 °2--1.6171 °2
S-0.2335 Å °1.861 Å °0.0095 Å °-0.367 Å °0.1749 Å °-0.2158 Å °0.2568 Å °-0.2394 Å °0.0587 Å °

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