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2lkn

Solution structure of the PPIase domain of human aryl-hydrocarbon receptor-interacting protein (AIP)

Method: SOLUTION NMR Dmax: 62.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

AH receptor-interacting protein

Homo sapiens

UniProt O00170

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 2–166 Fragment：PPIase FKBP-type domain containing residues 1-166 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7.5；298 K；Ionic strength (raw mmCIF value) 10；Pressure ambient NMR sample composition：2 mM AIP, 10 mM sodium phosphate, 5 mM DTT, 0.05 mM sodium azide, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition：2 mM [U-15N] AIP, 10 mM sodium phosphate, 5 mM DTT, 0.05 mM sodium azide, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition：2 mM [U-13C; U-15N] AIP, 10 mM sodium phosphate, 5 mM DTT, 0.05 mM sodium azide, 95% H2O/5% D2O | 95% H2O/5% 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 2LKN Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
4AIF AIP TPR domain in complex with human Hsp90 peptide Deposited 2012-02-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 172–315（144 aa） Fragment：TETRATRICOPEPTIDE DOMAIN, RESIDUES 172-315
Mutation：YES SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions 1 M AMMONIUM SULFATE, 0.1 M BIS-TRIS PH 5.5, 1% PEG 3350
Resolution 2.01 Å R-free 0.236
4AIF AIP TPR domain in complex with human Hsp90 peptide Deposited 2012-02-09 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 172–315（144 aa） Fragment：TETRATRICOPEPTIDE DOMAIN, RESIDUES 172-315
Mutation：YES No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions 1 M AMMONIUM SULFATE, 0.1 M BIS-TRIS PH 5.5, 1% PEG 3350
Resolution 2.01 Å R-free 0.236
4APO AIP TPR domain in complex with human Tomm20 peptide Deposited 2012-04-04 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 166–330（165 aa） Fragment：TETRATRICOPEPTIDE REPEAT DOMAIN, RESIDUES 172-313
Mutation：YES No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions PEG 3350, AMMONIUM SULFATE, BIS-TRIS PH 5.5
Resolution 1.90 Å R-free 0.234
4APO AIP TPR domain in complex with human Tomm20 peptide Deposited 2012-04-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 166–330（165 aa） Fragment：TETRATRICOPEPTIDE REPEAT DOMAIN, RESIDUES 172-313
Mutation：YES 12P DODECAETHYLENE GLYCOL × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions PEG 3350, AMMONIUM SULFATE, BIS-TRIS PH 5.5
Resolution 1.90 Å R-free 0.234
7ZUB Cryo-EM structure of the indirubin-bound Hsp90-XAP2-AHR complex Deposited 2022-05-12 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–330（330 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 MOO MOLYBDATE ION × 2 JY6 (3~{Z})-3-(3-oxidanylidene-1~{H}-indol-2-ylidene)-1~{H}-indol-2-one × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.85 Å
8QMO Cryo-EM structure of the benzo[a]pyrene-bound Hsp90-XAP2-AHR complex Deposited 2023-09-24 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–330（330 aa）
Not recorded MOO MOLYBDATE ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 W62 benzo[a]pyrene × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.76 Å

4 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AIP_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–165； UniProt 2–166

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 2lkn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2lkn
Deposition date deposition_date2011-10-17
Structure title titleSolution structure of the PPIase domain of human aryl-hydrocarbon receptor-interacting protein (AIP)
Keywords keywordsFKBP-TYPE DOMAIN, IMMUNOPHILIN HOMOLOG, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier17.77 Å
Radius of gyration Rg (electron density) rg_electron16.89 Å
Forward intensity I(0) i02017340000.00
Molecular weight molecular_weight372530.0 kDa
Excluded volume excluded_volume463160 ų
Envelope volume envelope_volume55207 ų
Hydration-shell volume shell_volume21923 ų
Envelope diameter envelope_diameter70.8 Å
Shell Rg shell_rg28.22 Å
Envelope Rg envelope_rg22.20 Å
Shape Rg shape_rg16.85 Å
Total Rg total_rg17.22 Å
Total atoms total_atoms52160
Residues n_residues3300
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 dmax62.5 Å
Rg (real space) rg_real17.76 Å
Rg uncertainty (real space) rg_real_error0.49 Å
I(0) (real space) i0_real2.0170e+09
I(0) uncertainty (real space) i0_real_error2.7030e+07
Rg (reciprocal space) rg_reciprocal17.76 Å
I(0) (reciprocal space) i0_reciprocal2017000000.0000
Solution quality estimate total_estimate0.7763
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.6 Å
Skewness Skewness skewness0.360
Kurtosis Kurtosis kurtosis-0.116
Angular range angular_range— – 0.4500 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1029000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.713; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.951; Smooth: 0.000
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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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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2lknA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology50 — Chitinase A; domain 3
Homologous superfamily homologous superfamily40 —
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8. Citations (1)

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9. Files and Curves (10)