2kxh

Solution structure of the first two RRM domains of FIR in the complex with FBP Nbox peptide

Method: SOLUTION NMR Dmax: 65.5 Å Quality: REASONABLE

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

Poly(U)-binding-splicing factor PUF60

Homo sapiens

UniProt Q9UHX1

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 119–314 Fragment:UNP residues 119-314 peptide of Far upstream element-binding protein 1 × 1 (Q96AE4) SOLUTION NMR NMR measurement conditions:pH 8;310 K;Ionic strength (raw mmCIF value) 0.06;Pressure ambient NMR measurement conditions:pH 8;318 K;Ionic strength (raw mmCIF value) 0.06;Pressure ambient NMR sample composition:0.6 mM [U-15N] protein_1-1, 10 mM TRIS-HCl pH 8.0-2, 50 mM sodium chloride-3, 2 mM TCEP-4, 1.25 mM protein_2-5, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:mM [U-13C; U-15N] protein_1-6, 10 mM TRIS-HCl pH 8.0-7, 50 mM sodium chloride-8, 2 mM TCEP-9, mM protein_2-10, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.3 mM [U-13C; U-15N] protein_2-11, 10 mM TRIS-HCl pH 8.0-12, 50 mM sodium chloride-13, 2 mM TCEP-14, mM protein_1-15, 100% D2O | 100% D2O NMR sample composition:mM [U-13C; U-15N] protein_1-16, 10 mM TRIS-HCl pH 8.0-17, 50 mM sodium chloride-18, 2 mM TCEP-19, mM protein_2-20, 100% D2O | 100% 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.

13 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PUF60_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–199; UniProt 119–314

peptide of Far upstream element-binding protein 1

Homo sapiens

UniProt Q96AE4

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 27–52 Fragment:UNP residues 27-52 Poly(U)-binding-splicing factor PUF60 × 1 (Q9UHX1) SOLUTION NMR NMR measurement conditions:pH 8;310 K;Ionic strength (raw mmCIF value) 0.06;Pressure ambient NMR measurement conditions:pH 8;318 K;Ionic strength (raw mmCIF value) 0.06;Pressure ambient NMR sample composition:0.6 mM [U-15N] protein_1-1, 10 mM TRIS-HCl pH 8.0-2, 50 mM sodium chloride-3, 2 mM TCEP-4, 1.25 mM protein_2-5, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:mM [U-13C; U-15N] protein_1-6, 10 mM TRIS-HCl pH 8.0-7, 50 mM sodium chloride-8, 2 mM TCEP-9, mM protein_2-10, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.3 mM [U-13C; U-15N] protein_2-11, 10 mM TRIS-HCl pH 8.0-12, 50 mM sodium chloride-13, 2 mM TCEP-14, mM protein_1-15, 100% D2O | 100% D2O NMR sample composition:mM [U-13C; U-15N] protein_1-16, 10 mM TRIS-HCl pH 8.0-17, 50 mM sodium chloride-18, 2 mM TCEP-19, mM protein_2-20, 100% D2O | 100% 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.

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

View Construct and Data Evidence
UniProt name FUBP1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–31; UniProt 27–52

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 2kxh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2kxh
Deposition date deposition_date2010-05-05
Structure title titleSolution structure of the first two RRM domains of FIR in the complex with FBP Nbox peptide
Keywords keywordsRRM, FIR, FBP, protein-protein complex, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier19.33
Radius of gyration Rg (electron density) rg_electron18.86
Forward intensity I(0) i03548720000.00
Molecular weight molecular_weight501130.0 kDa
Excluded volume excluded_volume625220 ų
Envelope volume envelope_volume78819 ų
Hydration-shell volume shell_volume28078 ų
Envelope diameter envelope_diameter72.4
Shell Rg shell_rg30.72
Envelope Rg envelope_rg23.24
Shape Rg shape_rg18.81
Total Rg total_rg19.20
Total atoms total_atoms70200
Residues n_residues4600
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 dmax65.5
Rg (real space) rg_real19.27
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real3.5490e+09
I(0) uncertainty (real space) i0_real_error4.8250e+07
Rg (reciprocal space) rg_reciprocal19.28
I(0) (reciprocal space) i0_reciprocal3549000000.0000
Solution quality estimate total_estimate0.7314
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.2
Skewness Skewness skewness0.229
Kurtosis Kurtosis kurtosis-0.434
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2139000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.822; Stabil: 1.000; Sysdev: 0.356; Positv: 1.000; Valcen: 0.977; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2kxha1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.7 — RNA-binding domain, RBD, aka RNA recognition motif (RRM)
Family Family familyd.58.7.0 — automated matches
Domain ID domain_idd2kxha2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.7 — RNA-binding domain, RBD, aka RNA recognition motif (RRM)
Family Family familyd.58.7.0 — automated matches
Domain ID domain_idd2kxha3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id2kxhA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain
Domain ID domain_id2kxhA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain

8. Citations (1)

9. Files and Curves (10)