5mk2

Crystal structure of the His Domain Protein Tyrosine Phosphatase (HD-PTP/PTPN23) Bro1 domain (CHMP4B peptide complex structure)

Method: X-RAY DIFFRACTION Dmax: 121.1 Å Quality: GOOD

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

Tyrosine-protein phosphatase non-receptor type 23

Homo sapiens

UniProt Q9H3S7

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–361 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.4;277 K;0.2 M CaCl2, 0.1 M MES pH 6.0, 20% PEG 6K Resolution 1.70 Å R-free 0.203
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–361 Not recorded Charged multivesicular body protein 4b × 1 (Q9H444) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.4;277 K;0.2 M CaCl2, 0.1 M MES pH 6.0, 20% PEG 6K Resolution 1.70 Å R-free 0.203

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.

10 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTN23_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–361; UniProt 1–361 Author chain B; PDBConstruct 1–361; UniProt 1–361

Charged multivesicular body protein 4b

OrganismNot specified

UniProt Q9H444

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 205–224 Not recorded Tyrosine-protein phosphatase non-receptor type 23 × 1 (Q9H3S7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.4;277 K;0.2 M CaCl2, 0.1 M MES pH 6.0, 20% PEG 6K Resolution 1.70 Å R-free 0.203

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.

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHM4B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–20; UniProt 205–224

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 5mk2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5mk2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5mk2
Deposition date deposition_date2016-12-02
Structure title titleCrystal structure of the His Domain Protein Tyrosine Phosphatase (HD-PTP/PTPN23) Bro1 domain (CHMP4B peptide complex structure)
Keywords keywordsESCRT-III CHMP4B, Hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.10
Radius of gyration Rg (electron density) rg_electron31.87
Forward intensity I(0) i0102861000.00
Molecular weight molecular_weight81923.0 kDa
Excluded volume excluded_volume103110 ų
Envelope volume envelope_volume127430 ų
Hydration-shell volume shell_volume34800 ų
Envelope diameter envelope_diameter129.3
Shell Rg shell_rg36.79
Envelope Rg envelope_rg31.97
Shape Rg shape_rg31.88
Total Rg total_rg32.23
Total atoms total_atoms5757
Residues n_residues727
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 dmax121.1
Rg (real space) rg_real32.38
Rg uncertainty (real space) rg_real_error1.58
I(0) (real space) i0_real1.0290e+08
I(0) uncertainty (real space) i0_real_error1.6660e+06
Rg (reciprocal space) rg_reciprocal32.26
I(0) (reciprocal space) i0_reciprocal102900000.0000
Solution quality estimate total_estimate0.8148
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.6
Skewness Skewness skewness0.583
Kurtosis Kurtosis kurtosis0.071
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23830000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.621; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.739; Smooth: 0.986

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5mk2A00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily280 — alix/aip1 like domains
Domain ID domain_id5mk2B00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily280 — alix/aip1 like domains

8. Citations (1)

9. Files and Curves (10)