2qwp

Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the ADP*Pi form #2

Method: X-RAY DIFFRACTION Dmax: 91.5 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–394 Mutation:R171C Putative tyrosine-protein phosphatase auxilin × 1 (Q27974) PO4 PHOSPHATE ION × 1 NA SODIUM ION × 2 MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ACY ACETIC ACID × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:microbatch under oil;pH 8.5;289 K;PEG3350, Ammonium Acetate, pH 8.5, microbatch under oil, temperature 289K Resolution 1.75 Å R-free 0.243

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 1–394; UniProt 1–394

Putative tyrosine-protein phosphatase auxilin

Bos taurus

UniProt Q27974

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 813–904 Mutation:D876C Heat shock cognate 71 kDa protein × 1 (P19120) PO4 PHOSPHATE ION × 1 NA SODIUM ION × 2 MG MAGNESIUM ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ACY ACETIC ACID × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:microbatch under oil;pH 8.5;289 K;PEG3350, Ammonium Acetate, pH 8.5, microbatch under oil, temperature 289K Resolution 1.75 Å R-free 0.243

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 AUXI_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–92; UniProt 813–904

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 2qwp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2qwp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2qwp
Deposition date deposition_date2007-08-10
Structure title titleCrystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the ADP*Pi form #2
Keywords keywords;chaperone-cochaperone complex, ATP-binding, Nucleotide-binding, Nucleus, Phosphorylation, Stress response, Hydrolase, Protein phosphatase, SH3-binding, CHAPERONE ;; CHAPERONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.77
Radius of gyration Rg (electron density) rg_electron25.24
Forward intensity I(0) i049144000.00
Molecular weight molecular_weight53929.0 kDa
Excluded volume excluded_volume67360 ų
Envelope volume envelope_volume83207 ų
Hydration-shell volume shell_volume28219 ų
Envelope diameter envelope_diameter96.7
Shell Rg shell_rg31.80
Envelope Rg envelope_rg25.56
Shape Rg shape_rg25.26
Total Rg total_rg25.92
Total atoms total_atoms3788
Residues n_residues478
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 dmax91.5
Rg (real space) rg_real25.84
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real4.9140e+07
I(0) uncertainty (real space) i0_real_error7.6620e+05
Rg (reciprocal space) rg_reciprocal25.82
I(0) (reciprocal space) i0_reciprocal49140000.0000
Solution quality estimate total_estimate0.8526
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.1
Skewness Skewness skewness0.493
Kurtosis Kurtosis kurtosis-0.015
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15990000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.714; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.946; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2qwpa1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.1 — Actin-like ATPase domain
Family Family familyc.55.1.1 — Actin/HSP70
Domain ID domain_idd2qwpa2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.1 — Actin-like ATPase domain
Family Family familyc.55.1.1 — Actin/HSP70
Domain ID domain_idd2qwpb_
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.3 — Chaperone J-domain
Family Family familya.2.3.1 — Chaperone J-domain

CATH v4.4 (5 domains)

Domain ID domain_id2qwpA01
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_id2qwpA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology30 — Defensin A-like
Homologous superfamily homologous superfamily30
Domain ID domain_id2qwpA03
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_id2qwpA04
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_id2qwpB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily110 — DnaJ domain

8. Citations (1)

9. Files and Curves (10)