1g9l

SOLUTION STRUCTURE OF THE PABC DOMAIN OF HUMAN POLY(A) BINDING PROTEIN

Method: SOLUTION NMR Dmax: 70.0 Å Quality: REASONABLE

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

POLYADENYLATE-BINDING PROTEIN 1

Homo sapiens

UniProt P11940

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 498–636 Fragment:C-TERMINAL DOMAIN (RESIDUES 498-636) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.3;303 K;Ionic strength (raw mmCIF value) 0.2;Pressure ambient NMR sample composition:3mM 15N-labeled PABC; 50mM phosphate buffer; 0.1M NaCl; 1mM NaN3; pH 6.3 | 90% H2O/10% D2O NMR sample composition:3mM 15N,13C-labeled PABC; 50mM phosphate buffer; 0.1M NaCl; 1mM NaN3; pH 6.3 | 100% D2O NMR sample composition:3mM unlabeled PABC; 50mM phosphate buffer; 0.1M NaCl; 1mM NaN3; pH 6.3 | 90% H2O/10% D2O Resolution not provided

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.

27 other PDB entries and 58 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PABP1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–144; UniProt 498–636

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 1g9l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1g9l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1g9l
Deposition date deposition_date2000-11-24
Structure title titleSOLUTION STRUCTURE OF THE PABC DOMAIN OF HUMAN POLY(A) BINDING PROTEIN
Keywords keywordsall-helical domain, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier26.65
Radius of gyration Rg (electron density) rg_electron26.82
Forward intensity I(0) i03070960000.00
Molecular weight molecular_weight458120.0 kDa
Excluded volume excluded_volume571640 ų
Envelope volume envelope_volume355960 ų
Hydration-shell volume shell_volume71508 ų
Envelope diameter envelope_diameter160.7
Shell Rg shell_rg46.57
Envelope Rg envelope_rg41.62
Shape Rg shape_rg26.88
Total Rg total_rg27.23
Total atoms total_atoms64770
Residues n_residues4320
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 dmax70.0
Rg (real space) rg_real24.29
Rg uncertainty (real space) rg_real_error0.20
I(0) (real space) i0_real2.9060e+09
I(0) uncertainty (real space) i0_real_error3.2460e+07
Rg (reciprocal space) rg_reciprocal27.16
I(0) (reciprocal space) i0_reciprocal3070000000.0000
Solution quality estimate total_estimate0.6482
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary17.5
Skewness Skewness skewness0.360
Kurtosis Kurtosis kurtosis-0.748
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha2.4450
Highest regularization parameter α highest_alpha942200.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.004; Oscil: 0.941; Stabil: 0.983; Sysdev: 0.000; Positv: 1.000; Valcen: 0.670; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1g9la1
Class classa — All alpha proteins
Fold Fold folda.144 — PABP domain-like
Superfamily Superfamily superfamilya.144.1 — PABC (PABP) domain
Family Family familya.144.1.1 — PABC (PABP) domain
Domain ID domain_idd1g9la2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1g9lA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1900 — c-terminal domain of poly(a) binding protein
Homologous superfamily homologous superfamily10 — c-terminal domain of poly(a) binding protein

8. Citations (1)

9. Files and Curves (10)