1bm5

THE SOLUTION STRUCTURE OF A SITE-DIRECTED MUTANT (R111M) OF HUMAN CELLULAR RETIONIC ACID BINDING PROTEIN-TYPE II, NMR, 31 STRUCTURES

Method: SOLUTION NMR Dmax: 45.8 Å Quality: GOOD

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

CELLULAR RETINOIC ACID BINDING PROTEIN-TYPE II

Homo sapiens

UniProt P29373

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 1–137 Mutation:R111M No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.3;300 K NMR sample composition:PBS 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.

84 other PDB entries and 138 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RABP2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–137; UniProt 1–137

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 1bm5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bm5
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1bm5
Deposition date deposition_date1998-07-28
Structure title titleTHE SOLUTION STRUCTURE OF A SITE-DIRECTED MUTANT (R111M) OF HUMAN CELLULAR RETIONIC ACID BINDING PROTEIN-TYPE II, NMR, 31 STRUCTURES
Keywords keywordsRETINOIC-ACID TRANSPORT, CRABPII; RETINOIC-ACID TRANSPORT
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.69
Radius of gyration Rg (electron density) rg_electron14.53
Forward intensity I(0) i03132530000.00
Molecular weight molecular_weight481550.0 kDa
Excluded volume excluded_volume604750 ų
Envelope volume envelope_volume36512 ų
Hydration-shell volume shell_volume17987 ų
Envelope diameter envelope_diameter53.1
Shell Rg shell_rg23.19
Envelope Rg envelope_rg16.81
Shape Rg shape_rg14.50
Total Rg total_rg14.69
Total atoms total_atoms67890
Residues n_residues4247
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 dmax45.8
Rg (real space) rg_real14.59
Rg uncertainty (real space) rg_real_error0.19
I(0) (real space) i0_real3.1330e+09
I(0) uncertainty (real space) i0_real_error3.2720e+07
Rg (reciprocal space) rg_reciprocal14.60
I(0) (reciprocal space) i0_reciprocal3133000000.0000
Solution quality estimate total_estimate0.8955
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.1
Skewness Skewness skewness0.124
Kurtosis Kurtosis kurtosis-0.371
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha739000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bm5a_
Class classb — All beta proteins
Fold Fold foldb.60 — Lipocalins
Superfamily Superfamily superfamilyb.60.1 — Lipocalins
Family Family familyb.60.1.2 — Fatty acid binding protein-like

CATH v4.4 (1 domains)

Domain ID domain_id1bm5A00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily20 — Calycin beta-barrel core domain

8. Citations (1)

9. Files and Curves (10)