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2l71

NMR solution structure of GIP in Bicellular media

Method: SOLUTION NMR Dmax: 58.7 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Gastric inhibitory polypeptide

OrganismNot specified

UniProt P09681

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 52–93 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 3.9；310 K NMR sample composition：100mM DHPC; 250mM DMPC; 90% H2O/10% D2O | 90% H2O/10% 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.

Other PDB Difference from Current Entry 2L71 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1T5Q Solution Structure of GIP(1-30)amide in TFE/Water Deposited 2004-05-05 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 52–81（30 aa） Fragment：residues 1-30
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3；298 K；Pressure ambient
NMR sample composition 2mM GIP(1-30)amide, 50% H2O, 50% d3-TFE | 50% H2O, 50% d3-TFE
Resolution not provided
2B4N Solution Structure of Glucose-Dependent Insulinotropic Polypeptide Deposited 2005-09-26 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 52–93（42 aa） Fragment：residues 52-93
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.3；298 K；Pressure AMBIENT
NMR sample composition 2mM GIP, 90% H2O, 10% D2O | 90% H2O/10% D2O
Resolution not provided
2L70 NMR solution structure of GIP in micellular media Deposited 2010-12-01 Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 52–93（42 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.9；310 K
NMR sample composition 150mM DHPC; 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2OBU Solution structure of GIP in TFE/water Deposited 2006-12-20 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 52–93（42 aa） Fragment：RESIDUES 52-93
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3；298 K；Pressure AMBIENT
NMR sample composition GIP, 50% TFE-D3, 50% H2O
Resolution not provided
2QKH Crystal structure of the extracellular domain of human GIP receptor in complex with the hormone GIP Deposited 2007-07-11 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 52–93（42 aa） Fragment：Sequence database residues 52-93
Not recorded TAR D(-)-TARTARIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；288 K；100 mM HEPES, 1 M potassium-sodium tartrate, 9% Methyl-beta-cyclodextrin, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 288K
Resolution 1.90 Å R-free 0.183
7DTY Structural basis of ligand selectivity conferred by the human glucose-dependent insulinotropic polypeptide receptor Deposited 2021-01-06 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain P 52–93（42 aa）
Not recorded CLR CHOLESTEROL × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.98 Å
7RA3 cryo-EM of human Gastric inhibitory polypeptide receptor GIPR bound to GIP Deposited 2021-06-29 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 7 PDB declaration: heptameric
Chain P 52–93（42 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.24 Å

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GIP_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–42； UniProt 52–93

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 2l71

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2l71
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2l71
Deposition date deposition_date2010-12-01
Structure title titleNMR solution structure of GIP in Bicellular media
Keywords keywordsGIP, Docking, Ala-scan, Type 2 diabetes, Hormone; HORMONE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier15.11 Å
Radius of gyration Rg (electron density) rg_electron15.44 Å
Forward intensity I(0) i079361000.00
Molecular weight molecular_weight74499.0 kDa
Excluded volume excluded_volume93279 ų
Envelope volume envelope_volume22778 ų
Hydration-shell volume shell_volume11884 ų
Envelope diameter envelope_diameter62.8 Å
Shell Rg shell_rg21.93 Å
Envelope Rg envelope_rg18.00 Å
Shape Rg shape_rg15.42 Å
Total Rg total_rg15.81 Å
Total atoms total_atoms10320
Residues n_residues630
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax58.7 Å
Rg (real space) rg_real15.45 Å
Rg uncertainty (real space) rg_real_error0.63 Å
I(0) (real space) i0_real7.9360e+07
I(0) uncertainty (real space) i0_real_error1.0190e+06
Rg (reciprocal space) rg_reciprocal15.42 Å
I(0) (reciprocal space) i0_reciprocal79360000.0000
Solution quality estimate total_estimate0.7084
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary9.7 Å
Skewness Skewness skewness0.542
Kurtosis Kurtosis kurtosis-0.469
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28730.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.387; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.046; Smooth: 0.999
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)