8t6f

Crystal structure of human MBP-Myeloid cell leukemia 1 (Mcl-1) in complex with BRD810 inhibitor

Method: X-RAY DIFFRACTION Dmax: 85.0 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Maltose/maltodextrin-binding periplasmic protein/Induced myeloid leukemia cell differentiation protein Mcl-1 Chimera

Homo sapiens

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 27–392 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 MG MAGNESIUM ION × 1 YI7 (3aM,9S,15R)-4-chloro-3-ethyl-7-{3-[(6-fluoronaphthalen-1-yl)oxy]propyl}-2-methyl-15-[2-(morpholin-4-yl)ethyl]-2,10,11,12,13,15-hexahydropyrazolo[4',3':9,10][1,6]oxazacycloundecino[8,7,6-hi]indole-8-carboxylic acid × 1 DMS DIMETHYL SULFOXIDE × 1 PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;3.75 mg/mL MBP-MCL1, 17.5 mM HEPES pH 7.5, 8% PEG 3350, 5% MPD, 5% DMSO, 2.5% PEG400, 75mM NaCl, 25mM Magnesium Formate, 0.75mM DTT, 0.75 mM Maltose, 0.5mM ANJ810, 0.375% glycerol, ~10-4 diluted microseeds, equilibrated against 1.5M NaCl in a EasyXtal 15-Well DropGuard Crystallization Tool Resolution 1.56 Å R-free 0.218

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–367; UniProt 27–392

Maltose/maltodextrin-binding periplasmic protein/Induced myeloid leukemia cell differentiation protein Mcl-1 Chimera

Homo sapiens

UniProt Q07820

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 174–321 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 MG MAGNESIUM ION × 1 YI7 (3aM,9S,15R)-4-chloro-3-ethyl-7-{3-[(6-fluoronaphthalen-1-yl)oxy]propyl}-2-methyl-15-[2-(morpholin-4-yl)ethyl]-2,10,11,12,13,15-hexahydropyrazolo[4',3':9,10][1,6]oxazacycloundecino[8,7,6-hi]indole-8-carboxylic acid × 1 DMS DIMETHYL SULFOXIDE × 1 PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;3.75 mg/mL MBP-MCL1, 17.5 mM HEPES pH 7.5, 8% PEG 3350, 5% MPD, 5% DMSO, 2.5% PEG400, 75mM NaCl, 25mM Magnesium Formate, 0.75mM DTT, 0.75 mM Maltose, 0.5mM ANJ810, 0.375% glycerol, ~10-4 diluted microseeds, equilibrated against 1.5M NaCl in a EasyXtal 15-Well DropGuard Crystallization Tool Resolution 1.56 Å R-free 0.218

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

141 other PDB entries and 285 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCL1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 371–518; UniProt 174–321

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8t6f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8t6f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8t6f
Deposition date deposition_date2023-06-15
Structure title titleCrystal structure of human MBP-Myeloid cell leukemia 1 (Mcl-1) in complex with BRD810 inhibitor
Keywords keywordsInhibitor, MCL1, MBP-fusion, BRD810, APOPTOSIS; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier26.17
Radius of gyration Rg (electron density) rg_electron25.22
Forward intensity I(0) i053805700.00
Molecular weight molecular_weight58516.0 kDa
Excluded volume excluded_volume73820 ų
Envelope volume envelope_volume86780 ų
Hydration-shell volume shell_volume28963 ų
Envelope diameter envelope_diameter86.9
Shell Rg shell_rg32.25
Envelope Rg envelope_rg25.19
Shape Rg shape_rg25.19
Total Rg total_rg26.09
Total atoms total_atoms4130
Residues n_residues518
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax85.0
Rg (real space) rg_real26.13
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real5.3810e+07
I(0) uncertainty (real space) i0_real_error7.4170e+05
Rg (reciprocal space) rg_reciprocal26.15
I(0) (reciprocal space) i0_reciprocal53810000.0000
Solution quality estimate total_estimate0.8968
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.9
Skewness Skewness skewness0.293
Kurtosis Kurtosis kurtosis-0.460
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17390000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.893; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)