5C8G

Crystal Structure Analysis of PP-BRD20 from Tb427tmp complexed with BI-2536

PDB DOI: https://doi.org/10.2210/pdb5C8G/pdb

Classification: GENE REGULATION
Organism(s): Trypanosoma brucei gambiense DAL972
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2015-06-25 Released: 2015-07-22
Deposition Author(s): Jiang, D.Q., Tempel, W., Loppnau, P., Graslund, S., Hou, C.F.D., El Bakkouri, M., Arrowsmith, C.H., Edwards, A.M., Bountra, C., Hui, R., Amain, M., Lin, Y.H., Structural Genomics Consortium (SGC)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.95 Å
R-Value Free: 0.240
R-Value Work: 0.193
R-Value Observed: 0.195

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 1.1 of the entry. See complete history.

Literature

Crystal Structure Analysis of PP-BRD20 from Tb427tmp

Jiang, D.Q., Tempel, W., Loppnau, P., Graslund, S., Hou, C.F.D., El Bakkouri, M., Arrowsmith, C.H., Edwards, A.M., Bountra, C., Hui, R., Amani, M., Lin, Y.H.

To be published.

Macromolecule Content

Total Structure Weight: 32.78 kDa
Atom Count: 2,086
Modelled Residue Count: 240
Deposited Residue Count: 272
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
PP-BRD20	A, B	136	Trypanosoma brucei gambiense DAL972	Mutation(s): 0 Gene Names: TbgDal_XI11310
UniProt
Find proteins for D0A8L1 (Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972)) Explore D0A8L1 Go to UniProtKB: D0A8L1
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	D0A8L1
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
R78 Query on R78 Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain O [auth B] MOL2 format, chain C [auth A] MOL2 format, chain O [auth B]	C [auth A], O [auth B]	4-{[(7R)-8-cyclopentyl-7-ethyl-5-methyl-6-oxo-5,6,7,8-tetrahydropteridin-2-yl]amino}-3-methoxy-N-(1-methylpiperidin-4-yl)benzamide C₂₈ H₃₉ N₇ O₃ XQVVPGYIWAGRNI-JOCHJYFZSA-N		Interactions Focus chain C [auth A] Focus chain O [auth B] Interactions & Density Focus chain C [auth A] Focus chain O [auth B]
UNX Query on UNX Download Ideal Coordinates CCD File SDF format, chain E [auth A] SDF format, chain F [auth A] SDF format, chain J [auth A] SDF format, chain K [auth A] SDF format, chain M [auth A] SDF format, chain N [auth A] SDF format, chain P [auth B] SDF format, chain Q [auth B] SDF format, chain D [auth A] SDF format, chain G [auth A] SDF format, chain H [auth A] SDF format, chain I [auth A] SDF format, chain L [auth A] MOL2 format, chain E [auth A] MOL2 format, chain F [auth A] MOL2 format, chain J [auth A] MOL2 format, chain K [auth A] MOL2 format, chain M [auth A] MOL2 format, chain N [auth A] MOL2 format, chain P [auth B] MOL2 format, chain Q [auth B] MOL2 format, chain D [auth A] MOL2 format, chain G [auth A] MOL2 format, chain H [auth A] MOL2 format, chain I [auth A] MOL2 format, chain L [auth A]	D [auth A] E [auth A] F [auth A] G [auth A] H [auth A] D [auth A], E [auth A], F [auth A], G [auth A], H [auth A], I [auth A], J [auth A], K [auth A], L [auth A], M [auth A], N [auth A], P [auth B], Q [auth B]	UNKNOWN ATOM OR ION X		Interactions Focus chain D [auth A] Focus chain E [auth A] Focus chain F [auth A] Focus chain G [auth A] Focus chain H [auth A] Focus chain I [auth A] Focus chain J [auth A] Focus chain K [auth A] Focus chain L [auth A] Focus chain M [auth A] Focus chain N [auth A] Focus chain P [auth B] Focus chain Q [auth B] Interactions & Density Focus chain D [auth A] Focus chain E [auth A] Focus chain F [auth A] Focus chain G [auth A] Focus chain H [auth A] Focus chain I [auth A] Focus chain J [auth A] Focus chain K [auth A] Focus chain L [auth A] Focus chain M [auth A] Focus chain N [auth A] Focus chain P [auth B] Focus chain Q [auth B]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.95 Å
R-Value Free: 0.240
R-Value Work: 0.193
R-Value Observed: 0.195
Space Group: P 4₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 53.092	α = 90
b = 53.092	β = 90
c = 103.424	γ = 90

Software Package:

Software Name	Purpose
HKL-2000	data scaling
PHENIX	refinement
PDB_EXTRACT	data extraction
HKL-3000	data reduction
PHASER	phasing

Structure Validation

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Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 2015-07-22

Deposition Author(s):

Structural Genomics Consortium (SGC)

Revision History (Full details and data files)

Version 1.0: 2015-07-22
Type: Initial release
Version 1.1: 2023-09-27
Changes: Data collection, Database references, Derived calculations, Refinement description, Source and taxonomy