[English] 日本語
Yorodumi
- PDB-3ffl: Crystal Structure of the N-terminal Domain of Anaphase-Promoting ... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3ffl
TitleCrystal Structure of the N-terminal Domain of Anaphase-Promoting Complex Subunit 7
ComponentsAnaphase-promoting complex subunit 7
KeywordsCELL CYCLE / Tetratricopeptide repeat motif / helis-turn-helix / Cell division / Mitosis / TPR repeat / Ubl conjugation pathway
Function / homology
Function and homology information


Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase / protein branched polyubiquitination / Inactivation of APC/C via direct inhibition of the APC/C complex / APC/C:Cdc20 mediated degradation of mitotic proteins / anaphase-promoting complex / Aberrant regulation of mitotic exit in cancer due to RB1 defects / regulation of meiotic cell cycle / anaphase-promoting complex-dependent catabolic process / Phosphorylation of the APC/C / positive regulation of mitotic metaphase/anaphase transition ...Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase / protein branched polyubiquitination / Inactivation of APC/C via direct inhibition of the APC/C complex / APC/C:Cdc20 mediated degradation of mitotic proteins / anaphase-promoting complex / Aberrant regulation of mitotic exit in cancer due to RB1 defects / regulation of meiotic cell cycle / anaphase-promoting complex-dependent catabolic process / Phosphorylation of the APC/C / positive regulation of mitotic metaphase/anaphase transition / protein K11-linked ubiquitination / enzyme-substrate adaptor activity / Regulation of APC/C activators between G1/S and early anaphase / Transcriptional Regulation by VENTX / protein K48-linked ubiquitination / heterochromatin / regulation of mitotic cell cycle / APC/C:Cdc20 mediated degradation of Cyclin B / APC-Cdc20 mediated degradation of Nek2A / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / Assembly of the pre-replicative complex / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / brain development / CDK-mediated phosphorylation and removal of Cdc6 / spindle / Separation of Sister Chromatids / microtubule cytoskeleton / Antigen processing: Ubiquitination & Proteasome degradation / Senescence-Associated Secretory Phenotype (SASP) / protein phosphatase binding / protein ubiquitination / cell division / nucleoplasm / nucleus / cytosol
Similarity search - Function
Tetratricopeptide repeat / Tetratricopeptide repeat domain / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Alpha Horseshoe / Tetratricopeptide-like helical domain superfamily / Mainly Alpha
Similarity search - Domain/homology
Anaphase-promoting complex subunit 7
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.5 Å
AuthorsHan, D. / Kim, K. / Kim, Y. / Kim, Y.
CitationJournal: To be published
Title: Crystal Structure of the N-terminal Domain of Anaphase-Promoting Complex Subunit 7
Authors: Han, D. / Kim, K. / Kim, Y. / Kang, Y. / Kim, Y.
History
DepositionDec 3, 2008Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Dec 16, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Apr 11, 2012Group: Refinement description
Revision 1.3Nov 10, 2021Group: Database references / Category: database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Anaphase-promoting complex subunit 7
B: Anaphase-promoting complex subunit 7
C: Anaphase-promoting complex subunit 7
D: Anaphase-promoting complex subunit 7


Theoretical massNumber of molelcules
Total (without water)74,8584
Polymers74,8584
Non-polymers00
Water86548
1
A: Anaphase-promoting complex subunit 7
C: Anaphase-promoting complex subunit 7


Theoretical massNumber of molelcules
Total (without water)37,4292
Polymers37,4292
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1100 Å2
ΔGint-13 kcal/mol
Surface area13980 Å2
MethodPISA
2
B: Anaphase-promoting complex subunit 7
D: Anaphase-promoting complex subunit 7


Theoretical massNumber of molelcules
Total (without water)37,4292
Polymers37,4292
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1170 Å2
ΔGint-14 kcal/mol
Surface area13740 Å2
MethodPISA
Unit cell
Length a, b, c (Å)80.493, 64.076, 81.597
Angle α, β, γ (deg.)90.00, 95.23, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein
Anaphase-promoting complex subunit 7 / APC7 / Cyclosome subunit 7


Mass: 18714.484 Da / Num. of mol.: 4 / Fragment: N-terminal domain / Mutation: M49L, M128L, M134V, M160L
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ANAPC7, APC7 / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) RIL / References: UniProt: Q9UJX3
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 48 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 3

-
Sample preparation

CrystalDensity Matthews: 2.8 Å3/Da / Density % sol: 56.06 %
Crystal growTemperature: 294 K / Method: vapor diffusion, sitting drop / pH: 8
Details: 0.2M sodium/potassium tartrate, 15% PEG 3350, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 294K

-
Data collection

Diffraction
IDCrystal-ID
11
21
31
Diffraction source
SourceSiteBeamlineIDWavelength (Å)
SYNCHROTRONPAL/PLS 4A10.97950, 0.97956, 0.97171
SYNCHROTRONPAL/PLS 6B20.97950, 0.97956, 0.97171
SYNCHROTRONPAL/PLS 6C130.97950, 0.97956, 0.97171
Detector
TypeIDDetectorDate
ADSC QUANTUM 2101CCDApr 2, 2008
ADSC QUANTUM 2102CCDOct 15, 2007
ADSC QUANTUM 2103CCDMar 16, 2008
Radiation
IDProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1MADMx-ray1
2MADMx-ray1
3MADMx-ray1
Radiation wavelength
IDWavelength (Å)Relative weight
10.97951
20.979561
30.971711
ReflectionResolution: 2.5→41.5 Å / Num. obs: 24411 / % possible obs: 100 %
Reflection shellResolution: 2.5→2.565 Å / Num. unique all: 1214 / % possible all: 100

-
Processing

Software
NameVersionClassification
ADSCQuantumdata collection
SOLVEphasing
REFMAC5.4.0067refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MAD / Resolution: 2.5→41 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.934 / SU B: 23.89 / SU ML: 0.235 / TLS residual ADP flag: UNVERIFIED / Cross valid method: THROUGHOUT / ESU R: 0.386 / ESU R Free: 0.249 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.24012 1300 5.1 %RANDOM
Rwork0.21647 ---
obs0.21768 24411 100 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 26.414 Å2
Baniso -1Baniso -2Baniso -3
1-0.25 Å20 Å2-0.08 Å2
2---0.82 Å20 Å2
3---0.55 Å2
Refinement stepCycle: LAST / Resolution: 2.5→41 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3997 0 0 48 4045
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.0224065
X-RAY DIFFRACTIONr_angle_refined_deg0.8221.9915493
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.1345492
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.70724.773176
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.20415769
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.971520
X-RAY DIFFRACTIONr_chiral_restr0.050.2640
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0212956
X-RAY DIFFRACTIONr_mcbond_it0.1831.52508
X-RAY DIFFRACTIONr_mcangle_it0.35924048
X-RAY DIFFRACTIONr_scbond_it0.52831557
X-RAY DIFFRACTIONr_scangle_it0.8934.51445
LS refinement shellResolution: 2.5→2.565 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.45 59 -
Rwork0.339 1214 -
obs--100 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
14.0892-0.52913.17795.12892.631114.54930.26380.4809-0.4342-0.90520.1139-0.15130.56550.0455-0.37780.56190.034-0.08370.3687-0.03410.12445.426-0.593-38.298
25.76730.42442.9088.65883.66515.31820.19090.0230.0016-0.7621-0.0303-0.11120.1798-0.2724-0.16060.2575-0.0186-0.03970.35110.02970.10186.474.263-25.453
36.79491.66633.53394.78812.099913.3654-0.0531-0.53280.4283-0.3747-0.027-0.1171-0.9826-0.0230.08010.19870.0007-0.00530.3487-0.05050.149411.29211.549-15.066
46.9284-2.1781-0.99968.9672.43615.3574-0.237-0.5814-0.2490.75030.4238-1.57270.45680.5028-0.18680.05030.0293-0.23590.73690.00850.572528.641-1.9012.978
58.3939-1.64890.22914.1711-0.11668.6141-0.0863-0.6752-0.19890.31930.0862-0.547-0.08390.05610.0001-0.015-0.0341-0.1230.5908-0.01450.131215.0413.6112.891
69.94730.72432.12165.94091.721510.04230.0313-0.59850.56640.37020.0335-0.0962-0.73790.072-0.06480.1359-0.0074-0.05560.6088-0.12670.12014.59210.7149.165
76.16350.65632.87684.5960.499611.43480.02290.6737-0.0295-1.11560.1506-0.13030.0940.7998-0.17350.4627-0.01910.01270.64270.09180.130411.58133.203-29.389
88.1709-1.32622.27247.41341.006110.71040.11570.34620.0358-0.5923-0.0193-0.36430.14330.6497-0.09640.1976-0.03960.00330.51920.10620.099412.54434.059-17.352
99.81730.42132.97514.87620.91388.1403-0.1981-0.28590.53910.00580.0888-0.3152-0.37570.42810.10930.1131-0.0491-0.04580.64490.05820.229317.3538.708-4.612
1016.160.8593.880811.0135-1.08617.9074-0.6505-1.32291.71741.3141-0.3577-2.7985-0.2945-0.20641.00820.2055-0.0339-0.32040.8692-0.15911.005142.06930.4778.418
1110.0425-2.79631.23218.3997-1.60994.0383-0.339-0.6686-0.48560.6390.647-0.46790.1444-0.5938-0.3080.01850.0163-0.1240.6985-0.01880.168529.36223.3068.151
1216.4661-2.15383.51396.1698-8.498713.1356-0.6202-3.30310.30352.77911.58631.2105-0.8584-1.6525-0.96610.73240.65670.37832.15320.34460.188216.72127.60421.831
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A21 - 74
2X-RAY DIFFRACTION2A75 - 133
3X-RAY DIFFRACTION3A134 - 166
4X-RAY DIFFRACTION4B21 - 72
5X-RAY DIFFRACTION5B73 - 136
6X-RAY DIFFRACTION6B137 - 166
7X-RAY DIFFRACTION7C22 - 68
8X-RAY DIFFRACTION8C69 - 124
9X-RAY DIFFRACTION9C125 - 166
10X-RAY DIFFRACTION10D22 - 41
11X-RAY DIFFRACTION11D42 - 142
12X-RAY DIFFRACTION12D143 - 165

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more