1qz2

Crystal Structure of FKBP52 C-terminal Domain complex with the C-terminal peptide MEEVD of Hsp90

Method: X-RAY DIFFRACTION Dmax: 110.8 Å Quality: EXCELLENT

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

FK506-binding protein 4

Homo sapiens

UniProt Q02790

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 144–458 Chain B; UniProt 144–458 Chain C; UniProt 144–458 Fragment:FKBP52 C-terminal Domain 5-mer peptide from Heat shock protein HSP 90 × 2 (P08238) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;291 K;Sodium Citrate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.00 Å R-free 0.287

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.

11 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FKBP4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 22–336; UniProt 144–458 Author chain B; PDBConstruct 22–336; UniProt 144–458 Author chain C; PDBConstruct 22–336; UniProt 144–458

5-mer peptide from Heat shock protein HSP 90

OrganismNot specified

UniProt P08238

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 719–723 Chain H; UniProt 719–723 Not recorded FK506-binding protein 4 × 3 (Q02790) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;291 K;Sodium Citrate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.00 Å R-free 0.287

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.

29 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HS90B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–5; UniProt 719–723 Author chain H; PDBConstruct 1–5; UniProt 719–723

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 1qz2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1qz2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1qz2
Deposition date deposition_date2003-09-15
Structure title titleCrystal Structure of FKBP52 C-terminal Domain complex with the C-terminal peptide MEEVD of Hsp90
Keywords keywordsIsomerase, Rotamase, chaperone, Heat shock, ISOMERASE-CHAPERONE COMPLEX; ISOMERASE/CHAPERONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.84
Radius of gyration Rg (electron density) rg_electron37.00
Forward intensity I(0) i0156718000.00
Molecular weight molecular_weight99428.0 kDa
Excluded volume excluded_volume124240 ų
Envelope volume envelope_volume194650 ų
Hydration-shell volume shell_volume44069 ų
Envelope diameter envelope_diameter110.8
Shell Rg shell_rg43.99
Envelope Rg envelope_rg34.65
Shape Rg shape_rg36.99
Total Rg total_rg37.58
Total atoms total_atoms7004
Residues n_residues865
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 dmax110.8
Rg (real space) rg_real37.60
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real1.5670e+08
I(0) uncertainty (real space) i0_real_error2.1390e+06
Rg (reciprocal space) rg_reciprocal37.76
I(0) (reciprocal space) i0_reciprocal156700000.0000
Solution quality estimate total_estimate0.9074
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary60.7
Skewness Skewness skewness-0.077
Kurtosis Kurtosis kurtosis-0.870
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha9649000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.955; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.929

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 15 domains

SCOP 2.08 (9 domains)

Domain ID domain_idd1qz2a1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.8 — TPR-like
Family Family familya.118.8.1 — Tetratricopeptide repeat (TPR)
Domain ID domain_idd1qz2a2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.26 — FKBP-like
Superfamily Superfamily superfamilyd.26.1 — FKBP-like
Family Family familyd.26.1.1 — FKBP immunophilin/proline isomerase
Domain ID domain_idd1qz2a3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1qz2b1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.8 — TPR-like
Family Family familya.118.8.1 — Tetratricopeptide repeat (TPR)
Domain ID domain_idd1qz2b2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.26 — FKBP-like
Superfamily Superfamily superfamilyd.26.1 — FKBP-like
Family Family familyd.26.1.1 — FKBP immunophilin/proline isomerase
Domain ID domain_idd1qz2b3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1qz2c1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.8 — TPR-like
Family Family familya.118.8.1 — Tetratricopeptide repeat (TPR)
Domain ID domain_idd1qz2c2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.26 — FKBP-like
Superfamily Superfamily superfamilyd.26.1 — FKBP-like
Family Family familyd.26.1.1 — FKBP immunophilin/proline isomerase
Domain ID domain_idd1qz2c3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (6 domains)

Domain ID domain_id1qz2A01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology50 — Chitinase A; domain 3
Homologous superfamily homologous superfamily40
Domain ID domain_id1qz2A02
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain
Domain ID domain_id1qz2B01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology50 — Chitinase A; domain 3
Homologous superfamily homologous superfamily40
Domain ID domain_id1qz2B02
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain
Domain ID domain_id1qz2C01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology50 — Chitinase A; domain 3
Homologous superfamily homologous superfamily40
Domain ID domain_id1qz2C02
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain

8. Citations (1)

9. Files and Curves (10)