5bnb

Crystal structure of a Ube2S-ubiquitin conjugate

Method: X-RAY DIFFRACTION Dmax: 117.0 Å Quality: GOOD

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

Ubiquitin-conjugating enzyme E2 S

Homo sapiens

UniProt Q16763

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 1–156 Mutation:C118M Polyubiquitin-B × 1 (P0CG47) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.1M Tris, 20% PEG 4000 Resolution 2.49 Å R-free 0.304
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–156 Mutation:C118M Polyubiquitin-B × 1 (P0CG47) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.1M Tris, 20% PEG 4000 Resolution 2.49 Å R-free 0.304
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–156 Mutation:C118M Polyubiquitin-B × 1 (P0CG47) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.1M Tris, 20% PEG 4000 Resolution 2.49 Å R-free 0.304
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–156 Mutation:C118M Polyubiquitin-B × 1 (P0CG47) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.1M Tris, 20% PEG 4000 Resolution 2.49 Å R-free 0.304

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.

8 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBE2S_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–156; UniProt 1–156 Author chain B; PDBConstruct 1–156; UniProt 1–156 Author chain C; PDBConstruct 1–156; UniProt 1–156 Author chain D; PDBConstruct 1–156; UniProt 1–156

Polyubiquitin-B

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 G; UniProt 1–76 Mutation:G76C Ubiquitin-conjugating enzyme E2 S × 1 (Q16763) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.1M Tris, 20% PEG 4000 Resolution 2.49 Å R-free 0.304
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 1–76 Mutation:G76C Ubiquitin-conjugating enzyme E2 S × 1 (Q16763) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.1M Tris, 20% PEG 4000 Resolution 2.49 Å R-free 0.304
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–76 Mutation:G76C Ubiquitin-conjugating enzyme E2 S × 1 (Q16763) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.1M Tris, 20% PEG 4000 Resolution 2.49 Å R-free 0.304
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 1–76 Mutation:G76C Ubiquitin-conjugating enzyme E2 S × 1 (Q16763) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;0.1M Tris, 20% PEG 4000 Resolution 2.49 Å R-free 0.304

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 E; PDBConstruct 1–76; UniProt 1–76 Author chain F; PDBConstruct 1–76; UniProt 1–76 Author chain G; PDBConstruct 1–76; UniProt 1–76 Author chain I; PDBConstruct 1–76; 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 5bnb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5bnb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5bnb
Deposition date deposition_date2015-05-25
Structure title titleCrystal structure of a Ube2S-ubiquitin conjugate
Keywords keywordsubiquitin-conjugating enzyme, E2 enzyme, UBC domain, ubiquitination, cell cycle; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.42
Radius of gyration Rg (electron density) rg_electron35.24
Forward intensity I(0) i0116374000.00
Molecular weight molecular_weight87287.0 kDa
Excluded volume excluded_volume109780 ų
Envelope volume envelope_volume162170 ų
Hydration-shell volume shell_volume39688 ų
Envelope diameter envelope_diameter126.8
Shell Rg shell_rg40.15
Envelope Rg envelope_rg34.69
Shape Rg shape_rg35.26
Total Rg total_rg35.55
Total atoms total_atoms11950
Residues n_residues852
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 dmax117.0
Rg (real space) rg_real35.48
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real1.1640e+08
I(0) uncertainty (real space) i0_real_error2.0490e+06
Rg (reciprocal space) rg_reciprocal35.45
I(0) (reciprocal space) i0_reciprocal116400000.0000
Solution quality estimate total_estimate0.8778
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.0
Skewness Skewness skewness0.398
Kurtosis Kurtosis kurtosis-0.305
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10890000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.851

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (7 domains)

Domain ID domain_idd5bnba_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.20 — UBC-like
Superfamily Superfamily superfamilyd.20.1 — UBC-like
Family Family familyd.20.1.1 — UBC-related
Domain ID domain_idd5bnbb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.20 — UBC-like
Superfamily Superfamily superfamilyd.20.1 — UBC-like
Family Family familyd.20.1.1 — UBC-related
Domain ID domain_idd5bnbc_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.20 — UBC-like
Superfamily Superfamily superfamilyd.20.1 — UBC-like
Family Family familyd.20.1.1 — UBC-related
Domain ID domain_idd5bnbe_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related
Domain ID domain_idd5bnbf_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related
Domain ID domain_idd5bnbg_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related
Domain ID domain_idd5bnbi_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related

CATH v4.4 (2 domains)

Domain ID domain_id5bnbB00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology110 — Ubiquitin Conjugating Enzyme
Homologous superfamily homologous superfamily10 — Ubiquitin Conjugating Enzyme
Domain ID domain_id5bnbC00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology110 — Ubiquitin Conjugating Enzyme
Homologous superfamily homologous superfamily10 — Ubiquitin Conjugating Enzyme

8. Citations (1)

9. Files and Curves (10)