4fl9

Crystal Structure of bovine hsc70(aa1-554)E213A/D214A at 1.9A Resolution

Method: X-RAY DIFFRACTION Dmax: 97.7 Å Quality: GOOD

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

Heat shock cognate 71 kDa protein

Bos taurus

UniProt P19120

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 1–554 Fragment:UNP residues 1-554 Mutation:E213A, D214A TMO trimethylamine oxide × 2 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 7.5;291 K;PEG8000,TRIMETHYL AMINE OXIDE , pH 7.5, Microbatch, temperature 291K Resolution 1.90 Å R-free 0.232

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.

41 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HSP7C_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–554; UniProt 1–554

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 4fl9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4fl9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4fl9
Deposition date deposition_date2012-06-14
Structure title titleCrystal Structure of bovine hsc70(aa1-554)E213A/D214A at 1.9A Resolution
Keywords keywordsheat shock protein, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.74
Radius of gyration Rg (electron density) rg_electron28.39
Forward intensity I(0) i058377200.00
Molecular weight molecular_weight59457.0 kDa
Excluded volume excluded_volume74353 ų
Envelope volume envelope_volume92808 ų
Hydration-shell volume shell_volume29039 ų
Envelope diameter envelope_diameter104.7
Shell Rg shell_rg33.74
Envelope Rg envelope_rg28.46
Shape Rg shape_rg28.39
Total Rg total_rg28.90
Total atoms total_atoms8375
Residues n_residues539
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 dmax97.7
Rg (real space) rg_real28.89
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real5.8380e+07
I(0) uncertainty (real space) i0_real_error8.8340e+05
Rg (reciprocal space) rg_reciprocal28.83
I(0) (reciprocal space) i0_reciprocal58370000.0000
Solution quality estimate total_estimate0.8587
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.2
Skewness Skewness skewness0.533
Kurtosis Kurtosis kurtosis-0.139
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11600000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.804; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.854; Smooth: 0.892

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 5 domains

CATH v4.4 (5 domains)

Domain ID domain_id4fl9A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id4fl9A02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology30 — Defensin A-like
Homologous superfamily homologous superfamily30
Domain ID domain_id4fl9A03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id4fl9A04
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id4fl9A05
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology34 — Substrate Binding Domain Of DNAk; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Substrate Binding Domain Of DNAk; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)