7m2k

CDC34A-Ubiquitin-2ab inhibitor complex

Method: X-RAY DIFFRACTION Dmax: 105.8 Å Quality: EXCELLENT

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

Ubiquitin-conjugating enzyme E2 R1

Homo sapiens

UniProt P49427

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 7–184 Not recorded Ubiquitin × 1 (P0CG47) GZM 4-[(3',5'-dichloro[1,1'-biphenyl]-4-yl)methyl]-N-ethyl-1-(methoxyacetyl)piperidine-4-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1M HEPES pH 7.0 29% PEG3350 40 mM DL-Malic acid 5 mM DTT Resolution 2.47 Å R-free 0.276
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 7–184 Not recorded Ubiquitin × 1 (P0CG47) GZM 4-[(3',5'-dichloro[1,1'-biphenyl]-4-yl)methyl]-N-ethyl-1-(methoxyacetyl)piperidine-4-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1M HEPES pH 7.0 29% PEG3350 40 mM DL-Malic acid 5 mM DTT Resolution 2.47 Å R-free 0.276
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 7–184 Not recorded Ubiquitin × 1 (P0CG47) GZM 4-[(3',5'-dichloro[1,1'-biphenyl]-4-yl)methyl]-N-ethyl-1-(methoxyacetyl)piperidine-4-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1M HEPES pH 7.0 29% PEG3350 40 mM DL-Malic acid 5 mM DTT Resolution 2.47 Å R-free 0.276
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 7–184 Not recorded Ubiquitin × 1 (P0CG47) GZM 4-[(3',5'-dichloro[1,1'-biphenyl]-4-yl)methyl]-N-ethyl-1-(methoxyacetyl)piperidine-4-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1M HEPES pH 7.0 29% PEG3350 40 mM DL-Malic acid 5 mM DTT Resolution 2.47 Å R-free 0.276

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.

4 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UB2R1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–180; UniProt 7–184 Author chain C; PDBConstruct 3–180; UniProt 7–184 Author chain E; PDBConstruct 3–180; UniProt 7–184 Author chain G; PDBConstruct 3–180; UniProt 7–184

Ubiquitin

Homo sapiens

UniProt P0CG47

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–76 Not recorded Ubiquitin-conjugating enzyme E2 R1 × 1 (P49427) GZM 4-[(3',5'-dichloro[1,1'-biphenyl]-4-yl)methyl]-N-ethyl-1-(methoxyacetyl)piperidine-4-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1M HEPES pH 7.0 29% PEG3350 40 mM DL-Malic acid 5 mM DTT Resolution 2.47 Å R-free 0.276
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–76 Not recorded Ubiquitin-conjugating enzyme E2 R1 × 1 (P49427) GZM 4-[(3',5'-dichloro[1,1'-biphenyl]-4-yl)methyl]-N-ethyl-1-(methoxyacetyl)piperidine-4-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1M HEPES pH 7.0 29% PEG3350 40 mM DL-Malic acid 5 mM DTT Resolution 2.47 Å R-free 0.276
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 1–76 Not recorded Ubiquitin-conjugating enzyme E2 R1 × 1 (P49427) GZM 4-[(3',5'-dichloro[1,1'-biphenyl]-4-yl)methyl]-N-ethyl-1-(methoxyacetyl)piperidine-4-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1M HEPES pH 7.0 29% PEG3350 40 mM DL-Malic acid 5 mM DTT Resolution 2.47 Å R-free 0.276
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 1–76 Not recorded Ubiquitin-conjugating enzyme E2 R1 × 1 (P49427) GZM 4-[(3',5'-dichloro[1,1'-biphenyl]-4-yl)methyl]-N-ethyl-1-(methoxyacetyl)piperidine-4-carboxamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1M HEPES pH 7.0 29% PEG3350 40 mM DL-Malic acid 5 mM DTT Resolution 2.47 Å R-free 0.276

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.

278 other PDB entries and 426 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–80; UniProt 1–76 Author chain D; PDBConstruct 5–80; UniProt 1–76 Author chain F; PDBConstruct 5–80; UniProt 1–76 Author chain H; PDBConstruct 5–80; UniProt 1–76

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 7m2k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7m2k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7m2k
Deposition date deposition_date2021-03-16
Structure title titleCDC34A-Ubiquitin-2ab inhibitor complex
Keywords keywordsUbiquitin, Ube2R1, Ubiquitin conjugating enzyme, inhibitor, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.57
Radius of gyration Rg (electron density) rg_electron33.66
Forward intensity I(0) i0156510000.00
Molecular weight molecular_weight103500.0 kDa
Excluded volume excluded_volume130950 ų
Envelope volume envelope_volume179800 ų
Hydration-shell volume shell_volume44223 ų
Envelope diameter envelope_diameter107.0
Shell Rg shell_rg40.96
Envelope Rg envelope_rg32.55
Shape Rg shape_rg33.66
Total Rg total_rg34.27
Total atoms total_atoms7320
Residues n_residues950
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 dmax105.8
Rg (real space) rg_real34.41
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real1.5650e+08
I(0) uncertainty (real space) i0_real_error2.3000e+06
Rg (reciprocal space) rg_reciprocal34.51
I(0) (reciprocal space) i0_reciprocal156500000.0000
Solution quality estimate total_estimate0.9098
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.0
Skewness Skewness skewness0.083
Kurtosis Kurtosis kurtosis-0.617
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23530000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.965; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.934

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id7m2kB01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id7m2kD01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id7m2kF01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id7m2kH01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)