9pq7

MBP-Mcl1 in complex with ligand 21b

Method: X-RAY DIFFRACTION Dmax: 84.1 Å Quality: EXCELLENT

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

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

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 A1CMG 17-chloranyl-33-fluoranyl-12-[2-(2-methoxyethoxy)ethyl]-5,14,22-trimethyl-28-oxa-9-thia-5,6,12,13,24-pentazaheptacyclo[27.7.1.1^{4,7}.0^{11,15}.0^{16,21}.0^{20,24}.0^{30,35}]octatriaconta-1(36),4(38),6,11(15),13,16,18,20,22,29(37),30(35),31,33-tridecaene-23-carboxylic acid × 1 EDO 1,2-ETHANEDIOL × 1 FMT FORMIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;285 K;19% (w/v) PEG3350, 0.17M Magnesium formate Resolution 1.24 Å R-free 0.171

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

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 173–321 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 A1CMG 17-chloranyl-33-fluoranyl-12-[2-(2-methoxyethoxy)ethyl]-5,14,22-trimethyl-28-oxa-9-thia-5,6,12,13,24-pentazaheptacyclo[27.7.1.1^{4,7}.0^{11,15}.0^{16,21}.0^{20,24}.0^{30,35}]octatriaconta-1(36),4(38),6,11(15),13,16,18,20,22,29(37),30(35),31,33-tridecaene-23-carboxylic acid × 1 EDO 1,2-ETHANEDIOL × 1 FMT FORMIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;285 K;19% (w/v) PEG3350, 0.17M Magnesium formate Resolution 1.24 Å R-free 0.171

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 370–518; UniProt 173–321

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 9pq7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9pq7
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9pq7
Deposition date deposition_date2025-07-22
最后修订 last_revision2025-10-08
Structure title titleMBP-Mcl1 in complex with ligand 21b
Keywords keywords;Myeloid cell leukemia 1, Mcl-1, B-cell lymphoma 2, Bcl-2, BH3 mimetic, Protein-protein interaction, Modulator, Apoptosis, Cancer, Leukemia, Myeloma, Lymphoma, SIGNALING PROTEIN ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.07
Radius of gyration Rg (electron density) rg_electron25.30
Forward intensity I(0) i0104600000.00
Molecular weight molecular_weight54348.0 kDa
Excluded volume excluded_volume52836 ų
Envelope volume envelope_volume87797 ų
Hydration-shell volume shell_volume29149 ų
Envelope diameter envelope_diameter87.0
Shell Rg shell_rg32.41
Envelope Rg envelope_rg25.32
Shape Rg shape_rg25.26
Total Rg total_rg25.92
Total atoms total_atoms4128
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 dmax84.1
Rg (real space) rg_real26.03
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real1.0460e+08
I(0) uncertainty (real space) i0_real_error1.4160e+06
Rg (reciprocal space) rg_reciprocal26.04
I(0) (reciprocal space) i0_reciprocal104600000.0000
Solution quality estimate total_estimate0.9005
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.6
Skewness Skewness skewness0.289
Kurtosis Kurtosis kurtosis-0.481
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23460000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)