1h2t

Structure of the human nuclear cap-binding-complex (CBC) in complex with a cap analogue m7GpppG

Method: X-RAY DIFFRACTION Dmax: 101.4 Å Quality: GOOD

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

80 KDA NUCLEAR CAP BINDING PROTEIN

HOMO SAPIENS

UniProt Q09161

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 C; UniProt 20–652 Chain C; UniProt 702–790 Fragment:MIF4G DOMAIN, RESIDUES 20-653,701-790 Mutation:YES 20 KDA NUCLEAR CAP BINDING PROTEIN × 1 (P52298) GDP GUANOSINE-5'-DIPHOSPHATE × 1 7MG 7N-METHYL-8-HYDROGUANOSINE-5'-MONOPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;0.25 TO 1 % PEG 4000, 100 MM MES PH6, 75 TO 100 MM MAGNESIUM FORMATE, pH 6.00 Resolution 2.10 Å R-free 0.269

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.

17 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CB80_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–633; UniProt 20–652 Author chain C; PDBConstruct 635–723; UniProt 702–790

20 KDA NUCLEAR CAP BINDING PROTEIN

HOMO SAPIENS

UniProt P52298

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 Z; UniProt 1–156 Not recorded 80 KDA NUCLEAR CAP BINDING PROTEIN × 1 (Q09161) GDP GUANOSINE-5'-DIPHOSPHATE × 1 7MG 7N-METHYL-8-HYDROGUANOSINE-5'-MONOPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;0.25 TO 1 % PEG 4000, 100 MM MES PH6, 75 TO 100 MM MAGNESIUM FORMATE, pH 6.00 Resolution 2.10 Å R-free 0.269

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.

17 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CB20_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain Z; PDBConstruct 1–156; UniProt 1–156

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 1h2t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1h2t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1h2t
Deposition date deposition_date2002-08-16
Structure title titleStructure of the human nuclear cap-binding-complex (CBC) in complex with a cap analogue m7GpppG
Keywords keywordsM7GCAP, CAP-BINDING-COMPLEX, RNP DOMAIN, MIF4G DOMAIN, RNA MATURATION, RNA EXPORT, NUCLEAR PROTEIN, RNA-BINDING; NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.21
Radius of gyration Rg (electron density) rg_electron30.28
Forward intensity I(0) i0151973000.00
Molecular weight molecular_weight99343.0 kDa
Excluded volume excluded_volume124750 ų
Envelope volume envelope_volume153330 ų
Hydration-shell volume shell_volume41648 ų
Envelope diameter envelope_diameter110.3
Shell Rg shell_rg37.96
Envelope Rg envelope_rg30.29
Shape Rg shape_rg30.27
Total Rg total_rg30.97
Total atoms total_atoms6991
Residues n_residues850
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 dmax101.4
Rg (real space) rg_real31.14
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.5200e+08
I(0) uncertainty (real space) i0_real_error2.3080e+06
Rg (reciprocal space) rg_reciprocal31.17
I(0) (reciprocal space) i0_reciprocal152000000.0000
Solution quality estimate total_estimate0.8889
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.8
Skewness Skewness skewness0.304
Kurtosis Kurtosis kurtosis-0.309
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35590000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.889; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.887

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1h2tc1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.14 — MIF4G domain-like
Domain ID domain_idd1h2tc2
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.14 — MIF4G domain-like
Domain ID domain_idd1h2tc3
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.14 — MIF4G domain-like
Domain ID domain_idd1h2tz_
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.58.7.1 — Canonical RBD

CATH v4.4 (4 domains)

Domain ID domain_id1h2tC01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily180
Domain ID domain_id1h2tC02
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily180
Domain ID domain_id1h2tC03
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily180
Domain ID domain_id1h2tZ00
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 (2)

9. Files and Curves (10)