2nn6

Structure of the human RNA exosome composed of Rrp41, Rrp45, Rrp46, Rrp43, Mtr3, Rrp42, Csl4, Rrp4, and Rrp40

Method: X-RAY DIFFRACTION Dmax: 121.5 Å Quality: GOOD

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

Polymyositis/scleroderma autoantigen 1

Homo sapiens

UniProt Q86Y41

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 1–302 Not recorded Exosome complex exonuclease RRP41 × 1 (Q9NPD3) Exosome complex exonuclease RRP43 × 1 (Q96B26) Exosome complex exonuclease RRP46 × 1 (Q9NQT4) Exosome complex exonuclease RRP42 × 1 (Q15024) Exosome component 6 × 1 (Q5RKV6) Exosome complex exonuclease RRP40 × 1 (Q9NQT5) Exosome complex exonuclease RRP4 × 1 (Q13868) ;3'-5' exoribonuclease CSL4 homolog ; × 1 (Q9Y3B2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;4.5-8% w/v PEG4000, 0.1M Sodium citrate, 1 mM TCEP, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.35 Å R-free 0.344

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q86Y41_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 18–319; UniProt 1–302

Exosome complex exonuclease RRP41

Homo sapiens

UniProt Q9NPD3

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain B; UniProt 1–244 Not recorded Polymyositis/scleroderma autoantigen 1 × 1 (Q86Y41) Exosome complex exonuclease RRP43 × 1 (Q96B26) Exosome complex exonuclease RRP46 × 1 (Q9NQT4) Exosome complex exonuclease RRP42 × 1 (Q15024) Exosome component 6 × 1 (Q5RKV6) Exosome complex exonuclease RRP40 × 1 (Q9NQT5) Exosome complex exonuclease RRP4 × 1 (Q13868) ;3'-5' exoribonuclease CSL4 homolog ; × 1 (Q9Y3B2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;4.5-8% w/v PEG4000, 0.1M Sodium citrate, 1 mM TCEP, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.35 Å R-free 0.344

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 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXOS4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–249; UniProt 1–244

Exosome complex exonuclease RRP43

Homo sapiens

UniProt Q96B26

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain C; UniProt 1–276 Not recorded Polymyositis/scleroderma autoantigen 1 × 1 (Q86Y41) Exosome complex exonuclease RRP41 × 1 (Q9NPD3) Exosome complex exonuclease RRP46 × 1 (Q9NQT4) Exosome complex exonuclease RRP42 × 1 (Q15024) Exosome component 6 × 1 (Q5RKV6) Exosome complex exonuclease RRP40 × 1 (Q9NQT5) Exosome complex exonuclease RRP4 × 1 (Q13868) ;3'-5' exoribonuclease CSL4 homolog ; × 1 (Q9Y3B2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;4.5-8% w/v PEG4000, 0.1M Sodium citrate, 1 mM TCEP, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.35 Å R-free 0.344

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 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXOS8_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 3–278; UniProt 1–276

Exosome complex exonuclease RRP46

Homo sapiens

UniProt Q9NQT4

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain D; UniProt 1–235 Not recorded Polymyositis/scleroderma autoantigen 1 × 1 (Q86Y41) Exosome complex exonuclease RRP41 × 1 (Q9NPD3) Exosome complex exonuclease RRP43 × 1 (Q96B26) Exosome complex exonuclease RRP42 × 1 (Q15024) Exosome component 6 × 1 (Q5RKV6) Exosome complex exonuclease RRP40 × 1 (Q9NQT5) Exosome complex exonuclease RRP4 × 1 (Q13868) ;3'-5' exoribonuclease CSL4 homolog ; × 1 (Q9Y3B2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;4.5-8% w/v PEG4000, 0.1M Sodium citrate, 1 mM TCEP, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.35 Å R-free 0.344

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 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXOS5_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 3–237; UniProt 1–235

Exosome complex exonuclease RRP42

Homo sapiens

UniProt Q15024

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain E; UniProt 1–291 Mutation:L274V Polymyositis/scleroderma autoantigen 1 × 1 (Q86Y41) Exosome complex exonuclease RRP41 × 1 (Q9NPD3) Exosome complex exonuclease RRP43 × 1 (Q96B26) Exosome complex exonuclease RRP46 × 1 (Q9NQT4) Exosome component 6 × 1 (Q5RKV6) Exosome complex exonuclease RRP40 × 1 (Q9NQT5) Exosome complex exonuclease RRP4 × 1 (Q13868) ;3'-5' exoribonuclease CSL4 homolog ; × 1 (Q9Y3B2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;4.5-8% w/v PEG4000, 0.1M Sodium citrate, 1 mM TCEP, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.35 Å R-free 0.344

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 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXOS7_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 15–305; UniProt 1–291

Exosome component 6

Homo sapiens

UniProt Q5RKV6

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain F; UniProt 1–272 Not recorded Polymyositis/scleroderma autoantigen 1 × 1 (Q86Y41) Exosome complex exonuclease RRP41 × 1 (Q9NPD3) Exosome complex exonuclease RRP43 × 1 (Q96B26) Exosome complex exonuclease RRP46 × 1 (Q9NQT4) Exosome complex exonuclease RRP42 × 1 (Q15024) Exosome complex exonuclease RRP40 × 1 (Q9NQT5) Exosome complex exonuclease RRP4 × 1 (Q13868) ;3'-5' exoribonuclease CSL4 homolog ; × 1 (Q9Y3B2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;4.5-8% w/v PEG4000, 0.1M Sodium citrate, 1 mM TCEP, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.35 Å R-free 0.344

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 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q5RKV6_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–272; UniProt 1–272

Exosome complex exonuclease RRP40

Homo sapiens

UniProt Q9NQT5

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain G; UniProt 0–274 Not recorded Polymyositis/scleroderma autoantigen 1 × 1 (Q86Y41) Exosome complex exonuclease RRP41 × 1 (Q9NPD3) Exosome complex exonuclease RRP43 × 1 (Q96B26) Exosome complex exonuclease RRP46 × 1 (Q9NQT4) Exosome complex exonuclease RRP42 × 1 (Q15024) Exosome component 6 × 1 (Q5RKV6) Exosome complex exonuclease RRP4 × 1 (Q13868) ;3'-5' exoribonuclease CSL4 homolog ; × 1 (Q9Y3B2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;4.5-8% w/v PEG4000, 0.1M Sodium citrate, 1 mM TCEP, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.35 Å R-free 0.344

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 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXOS3_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 15–289; UniProt 0–274

Exosome complex exonuclease RRP4

Homo sapiens

UniProt Q13868

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain H; UniProt 1–293 Not recorded Polymyositis/scleroderma autoantigen 1 × 1 (Q86Y41) Exosome complex exonuclease RRP41 × 1 (Q9NPD3) Exosome complex exonuclease RRP43 × 1 (Q96B26) Exosome complex exonuclease RRP46 × 1 (Q9NQT4) Exosome complex exonuclease RRP42 × 1 (Q15024) Exosome component 6 × 1 (Q5RKV6) Exosome complex exonuclease RRP40 × 1 (Q9NQT5) ;3'-5' exoribonuclease CSL4 homolog ; × 1 (Q9Y3B2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;4.5-8% w/v PEG4000, 0.1M Sodium citrate, 1 mM TCEP, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.35 Å R-free 0.344

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 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXOS2_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 16–308; UniProt 1–293

;3'-5' exoribonuclease CSL4 homolog ;

Homo sapiens

UniProt Q9Y3B2

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain I; UniProt 1–195 Not recorded Polymyositis/scleroderma autoantigen 1 × 1 (Q86Y41) Exosome complex exonuclease RRP41 × 1 (Q9NPD3) Exosome complex exonuclease RRP43 × 1 (Q96B26) Exosome complex exonuclease RRP46 × 1 (Q9NQT4) Exosome complex exonuclease RRP42 × 1 (Q15024) Exosome component 6 × 1 (Q5RKV6) Exosome complex exonuclease RRP40 × 1 (Q9NQT5) Exosome complex exonuclease RRP4 × 1 (Q13868) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;4.5-8% w/v PEG4000, 0.1M Sodium citrate, 1 mM TCEP, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.35 Å R-free 0.344

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 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXOS1_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain I; PDBConstruct 15–209; UniProt 1–195

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 2nn6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2nn6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2nn6
Deposition date deposition_date2006-10-23
Structure title titleStructure of the human RNA exosome composed of Rrp41, Rrp45, Rrp46, Rrp43, Mtr3, Rrp42, Csl4, Rrp4, and Rrp40
Keywords keywordsRNA, exosome, PM/Scl, exoribonuclease, phosphorolytic, ribonuclease, HYDROLASE-TRANSFERASE COMPLEX; HYDROLASE/TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.50
Radius of gyration Rg (electron density) rg_electron39.74
Forward intensity I(0) i0871386000.00
Molecular weight molecular_weight240640.0 kDa
Excluded volume excluded_volume301280 ų
Envelope volume envelope_volume421650 ų
Hydration-shell volume shell_volume83650 ų
Envelope diameter envelope_diameter127.4
Shell Rg shell_rg49.30
Envelope Rg envelope_rg38.58
Shape Rg shape_rg39.74
Total Rg total_rg40.24
Total atoms total_atoms16858
Residues n_residues2214
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 dmax121.5
Rg (real space) rg_real40.22
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real8.7140e+08
I(0) uncertainty (real space) i0_real_error1.2740e+07
Rg (reciprocal space) rg_reciprocal40.49
I(0) (reciprocal space) i0_reciprocal871600000.0000
Solution quality estimate total_estimate0.8976
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.1
Skewness Skewness skewness-0.007
Kurtosis Kurtosis kurtosis-0.563
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha151700000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.922; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.958; Smooth: 0.942

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 32 domains

SCOP 2.08 (20 domains)

Domain ID domain_idd2nn6a1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.14 — Ribosomal protein S5 domain 2-like
Superfamily Superfamily superfamilyd.14.1 — Ribosomal protein S5 domain 2-like
Family Family familyd.14.1.4 — Ribonuclease PH domain 1-like
Domain ID domain_idd2nn6a2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.101 — Ribonuclease PH domain 2-like
Superfamily Superfamily superfamilyd.101.1 — Ribonuclease PH domain 2-like
Family Family familyd.101.1.1 — Ribonuclease PH domain 2-like
Domain ID domain_idd2nn6b1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.14 — Ribosomal protein S5 domain 2-like
Superfamily Superfamily superfamilyd.14.1 — Ribosomal protein S5 domain 2-like
Family Family familyd.14.1.4 — Ribonuclease PH domain 1-like
Domain ID domain_idd2nn6b2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.101 — Ribonuclease PH domain 2-like
Superfamily Superfamily superfamilyd.101.1 — Ribonuclease PH domain 2-like
Family Family familyd.101.1.1 — Ribonuclease PH domain 2-like
Domain ID domain_idd2nn6c1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.14 — Ribosomal protein S5 domain 2-like
Superfamily Superfamily superfamilyd.14.1 — Ribosomal protein S5 domain 2-like
Family Family familyd.14.1.4 — Ribonuclease PH domain 1-like
Domain ID domain_idd2nn6c2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.101 — Ribonuclease PH domain 2-like
Superfamily Superfamily superfamilyd.101.1 — Ribonuclease PH domain 2-like
Family Family familyd.101.1.1 — Ribonuclease PH domain 2-like
Domain ID domain_idd2nn6d1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.14 — Ribosomal protein S5 domain 2-like
Superfamily Superfamily superfamilyd.14.1 — Ribosomal protein S5 domain 2-like
Family Family familyd.14.1.4 — Ribonuclease PH domain 1-like
Domain ID domain_idd2nn6d2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.101 — Ribonuclease PH domain 2-like
Superfamily Superfamily superfamilyd.101.1 — Ribonuclease PH domain 2-like
Family Family familyd.101.1.1 — Ribonuclease PH domain 2-like
Domain ID domain_idd2nn6e1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.14 — Ribosomal protein S5 domain 2-like
Superfamily Superfamily superfamilyd.14.1 — Ribosomal protein S5 domain 2-like
Family Family familyd.14.1.4 — Ribonuclease PH domain 1-like
Domain ID domain_idd2nn6e2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.101 — Ribonuclease PH domain 2-like
Superfamily Superfamily superfamilyd.101.1 — Ribonuclease PH domain 2-like
Family Family familyd.101.1.1 — Ribonuclease PH domain 2-like
Domain ID domain_idd2nn6f1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.14 — Ribosomal protein S5 domain 2-like
Superfamily Superfamily superfamilyd.14.1 — Ribosomal protein S5 domain 2-like
Family Family familyd.14.1.4 — Ribonuclease PH domain 1-like
Domain ID domain_idd2nn6f2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.101 — Ribonuclease PH domain 2-like
Superfamily Superfamily superfamilyd.101.1 — Ribonuclease PH domain 2-like
Family Family familyd.101.1.1 — Ribonuclease PH domain 2-like
Domain ID domain_idd2nn6g1
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.4 — Nucleic acid-binding proteins
Family Family familyb.40.4.5 — Cold shock DNA-binding domain-like
Domain ID domain_idd2nn6g2
Class classb — All beta proteins
Fold Fold foldb.84 — Barrel-sandwich hybrid
Superfamily Superfamily superfamilyb.84.4 — Ribosomal L27 protein-like
Family Family familyb.84.4.2 — ECR1 N-terminal domain-like
Domain ID domain_idd2nn6g3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.51 — Eukaryotic type KH-domain (KH-domain type I)
Superfamily Superfamily superfamilyd.51.1 — Eukaryotic type KH-domain (KH-domain type I)
Family Family familyd.51.1.1 — Eukaryotic type KH-domain (KH-domain type I)
Domain ID domain_idd2nn6h1
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.4 — Nucleic acid-binding proteins
Family Family familyb.40.4.5 — Cold shock DNA-binding domain-like
Domain ID domain_idd2nn6h2
Class classb — All beta proteins
Fold Fold foldb.84 — Barrel-sandwich hybrid
Superfamily Superfamily superfamilyb.84.4 — Ribosomal L27 protein-like
Family Family familyb.84.4.2 — ECR1 N-terminal domain-like
Domain ID domain_idd2nn6h3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.51 — Eukaryotic type KH-domain (KH-domain type I)
Superfamily Superfamily superfamilyd.51.1 — Eukaryotic type KH-domain (KH-domain type I)
Family Family familyd.51.1.1 — Eukaryotic type KH-domain (KH-domain type I)
Domain ID domain_idd2nn6i1
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.4 — Nucleic acid-binding proteins
Family Family familyb.40.4.5 — Cold shock DNA-binding domain-like
Domain ID domain_idd2nn6i2
Class classb — All beta proteins
Fold Fold foldb.84 — Barrel-sandwich hybrid
Superfamily Superfamily superfamilyb.84.4 — Ribosomal L27 protein-like
Family Family familyb.84.4.2 — ECR1 N-terminal domain-like

CATH v4.4 (12 domains)

Domain ID domain_id2nn6A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily70 — GHMP Kinase, N-terminal domain
Domain ID domain_id2nn6B01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily70 — GHMP Kinase, N-terminal domain
Domain ID domain_id2nn6C00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily70 — GHMP Kinase, N-terminal domain
Domain ID domain_id2nn6D00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily70 — GHMP Kinase, N-terminal domain
Domain ID domain_id2nn6E00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily70 — GHMP Kinase, N-terminal domain
Domain ID domain_id2nn6F00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily70 — GHMP Kinase, N-terminal domain
Domain ID domain_id2nn6G01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily100 — RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain
Domain ID domain_id2nn6G02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins
Domain ID domain_id2nn6G03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1370 — Ribosomal Protein S8; Chain: A, domain 1
Homologous superfamily homologous superfamily10 — K Homology domain, type 1
Domain ID domain_id2nn6H01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily100 — RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain
Domain ID domain_id2nn6I01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily100 — RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain
Domain ID domain_id2nn6I02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins

8. Citations (1)

9. Files and Curves (10)