3ia3

A cis-proline in alpha-hemoglobin stabilizing Protein directs the structural reorganization of alpha-hemoglobin

Method: X-RAY DIFFRACTION Dmax: 101.0 Å Quality: GOOD

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

Alpha-hemoglobin-stabilizing protein

Homo sapiens

UniProt Q9NZD4

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 1–91 Not recorded Hemoglobin subunit alpha × 1 (P69905) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;0.1 M MES, pH 6.5, 4% acetonitrile and 14.5% (w/v) PEG3000, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.20 Å R-free 0.293
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–91 Not recorded Hemoglobin subunit alpha × 1 (P69905) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;0.1 M MES, pH 6.5, 4% acetonitrile and 14.5% (w/v) PEG3000, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.20 Å R-free 0.293

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.

7 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AHSP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–91; UniProt 1–91 Author chain C; PDBConstruct 1–91; UniProt 1–91

Hemoglobin subunit alpha

Homo sapiens

UniProt P69905

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 D; UniProt 1–142 Not recorded Alpha-hemoglobin-stabilizing protein × 1 (Q9NZD4) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;0.1 M MES, pH 6.5, 4% acetonitrile and 14.5% (w/v) PEG3000, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.20 Å R-free 0.293
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–142 Not recorded Alpha-hemoglobin-stabilizing protein × 1 (Q9NZD4) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;0.1 M MES, pH 6.5, 4% acetonitrile and 14.5% (w/v) PEG3000, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.20 Å R-free 0.293

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.

348 other PDB entries and 411 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HBA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–145; UniProt 1–142 Author chain D; PDBConstruct 4–145; UniProt 1–142

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 3ia3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ia3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ia3
Deposition date deposition_date2009-07-13
Structure title titleA cis-proline in alpha-hemoglobin stabilizing Protein directs the structural reorganization of alpha-hemoglobin
Keywords keywords;Hemoglobin, cis-proline, ahsp, stabilization, Chaperone, Cytoplasm, Polymorphism, Acetylation, Disease mutation, Glycation, Glycoprotein, Heme, Iron, Metal-binding, Oxygen transport, Phosphoprotein, Transport ;; OXYGEN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.29
Radius of gyration Rg (electron density) rg_electron28.06
Forward intensity I(0) i040744100.00
Molecular weight molecular_weight51060.0 kDa
Excluded volume excluded_volume64469 ų
Envelope volume envelope_volume80139 ų
Hydration-shell volume shell_volume25947 ų
Envelope diameter envelope_diameter104.8
Shell Rg shell_rg32.57
Envelope Rg envelope_rg28.33
Shape Rg shape_rg28.02
Total Rg total_rg28.68
Total atoms total_atoms3606
Residues n_residues450
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 dmax101.0
Rg (real space) rg_real28.66
Rg uncertainty (real space) rg_real_error1.10
I(0) (real space) i0_real4.0740e+07
I(0) uncertainty (real space) i0_real_error6.8590e+05
Rg (reciprocal space) rg_reciprocal28.55
I(0) (reciprocal space) i0_reciprocal40740000.0000
Solution quality estimate total_estimate0.8046
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.1
Skewness Skewness skewness0.631
Kurtosis Kurtosis kurtosis-0.061
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10530000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.643; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.639; Smooth: 0.888

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3ia3A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily420 — AHSP
Domain ID domain_id3ia3B00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology490 — Globin-like
Homologous superfamily homologous superfamily10 — Globins
Domain ID domain_id3ia3C00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily420 — AHSP
Domain ID domain_id3ia3D00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology490 — Globin-like
Homologous superfamily homologous superfamily10 — Globins

8. Citations (1)

9. Files and Curves (10)