2d7c

Crystal structure of human Rab11 in complex with FIP3 Rab-binding domain

Method: X-RAY DIFFRACTION Dmax: 85.2 Å Quality: GOOD

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

Ras-related protein Rab-11A

Homo sapiens

UniProt P62491

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 6–172 Fragment:residues 7-173 Mutation:Q70L Non-standard monomer:Yes (specific site not provided by mmCIF) Rab11 family-interacting protein 3 × 1 (O75154) MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;289 K;20% iso-propanol, 3% (w/v) PEG 4000, 0.05M MES-NaOH, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 1.75 Å R-free 0.224
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 6–172 Fragment:residues 7-173 Mutation:Q70L Non-standard monomer:Yes (specific site not provided by mmCIF) Rab11 family-interacting protein 3 × 1 (O75154) MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;289 K;20% iso-propanol, 3% (w/v) PEG 4000, 0.05M MES-NaOH, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 1.75 Å R-free 0.224

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.

26 other PDB entries and 57 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RB11A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–167; UniProt 6–172 Author chain B; PDBConstruct 1–167; UniProt 6–172

Rab11 family-interacting protein 3

Homo sapiens

UniProt O75154

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 715–756 Fragment:Rab-binding domain Non-standard monomer:Yes (specific site not provided by mmCIF) Ras-related protein Rab-11A × 1 (P62491) MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;289 K;20% iso-propanol, 3% (w/v) PEG 4000, 0.05M MES-NaOH, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 1.75 Å R-free 0.224
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 715–756 Fragment:Rab-binding domain Non-standard monomer:Yes (specific site not provided by mmCIF) Ras-related protein Rab-11A × 1 (P62491) MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;289 K;20% iso-propanol, 3% (w/v) PEG 4000, 0.05M MES-NaOH, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 1.75 Å R-free 0.224

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.

4 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFIP3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–42; UniProt 715–756 Author chain D; PDBConstruct 1–42; UniProt 715–756

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 2d7c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2d7c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2d7c
Deposition date deposition_date2005-11-16
Structure title titleCrystal structure of human Rab11 in complex with FIP3 Rab-binding domain
Keywords keywordsGTP-ase, coiled-coil, PROTEIN TRANSPORT, Structural Genomics; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.26
Radius of gyration Rg (electron density) rg_electron26.69
Forward intensity I(0) i042228900.00
Molecular weight molecular_weight49150.0 kDa
Excluded volume excluded_volume60986 ų
Envelope volume envelope_volume74805 ų
Hydration-shell volume shell_volume24633 ų
Envelope diameter envelope_diameter88.6
Shell Rg shell_rg32.59
Envelope Rg envelope_rg26.48
Shape Rg shape_rg26.72
Total Rg total_rg27.25
Total atoms total_atoms3434
Residues n_residues412
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 dmax85.2
Rg (real space) rg_real27.39
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real4.2230e+07
I(0) uncertainty (real space) i0_real_error5.4860e+05
Rg (reciprocal space) rg_reciprocal27.35
I(0) (reciprocal space) i0_reciprocal42230000.0000
Solution quality estimate total_estimate0.8865
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.4
Skewness Skewness skewness0.390
Kurtosis Kurtosis kurtosis-0.594
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5703000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.932; Smooth: 0.851

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2d7ca_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd2d7cb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd2d7cc1
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.31 — Eferin C-derminal domain-like
Family Family familyh.1.31.1 — Eferin C-derminal domain-like
Domain ID domain_idd2d7cd_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.31 — Eferin C-derminal domain-like
Family Family familyh.1.31.1 — Eferin C-derminal domain-like

CATH v4.4 (4 domains)

Domain ID domain_id2d7cA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id2d7cB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id2d7cC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily2440
Domain ID domain_id2d7cD00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily2440

8. Citations (1)

9. Files and Curves (10)