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1tgr

Crystal Structure of mini-IGF-1(2)

Method: X-RAY DIFFRACTION Dmax: 52.3 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Insulin-like growth factor IA

Homo sapiens

UniProt P01343

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 49–77 Chain A； UniProt 90–110 Fragment：residues 1-52 Mutation：T29K No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.65；289 K；Citrate, ethanol, pH 6.65, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 1.42 Å R-free 0.224
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 49–77 Chain B； UniProt 90–110 Fragment：residues 1-52 Mutation：T29K No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.65；289 K；Citrate, ethanol, pH 6.65, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 1.42 Å R-free 0.224
3 Protein homooligomer Homooligomer Protein × 8 PDB declaration: octameric（8） Consistent with protein copy count Chain A； UniProt 49–77 Chain A； UniProt 90–110 Chain B； UniProt 49–77 Chain B； UniProt 90–110 Fragment：residues 1-52 Mutation：T29K No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.65；289 K；Citrate, ethanol, pH 6.65, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 1.42 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.

Other PDB Difference from Current Entry 1TGR Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1B9G INSULIN-LIKE-GROWTH-FACTOR-1 Deposited 1999-02-11 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–57（57 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 1.9；293 K
Resolution not provided
1GZR Human Insulin-like growth factor; ESRF data Deposited 2002-05-28 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 49–118（70 aa）
Not recorded C15 N-DODECYL-N,N-DIMETHYL-3-AMMONIO-1-PROPANESULFONATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；THE PROTEIN WAS CRYSTALLIZED BY THE HANGING DROP METHOD IN WHICH DROPS WERE COMPOSED OF VARIOUS RATIOS OF HIGF-I AT 7MG/ML (IN H2O) WITH RESERVOIR SOLUTION CONSISTING OF 0.1M TRIS.HCL PH 7.5, 12-15% (W/V) PEG 2K AND 5MM SB12 DETERGENT.
Resolution 2.00 Å R-free 0.295
1GZY Human Insulin-like growth factor; In-house data Deposited 2002-06-10 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 49–118（70 aa）
Not recorded C15 N-DODECYL-N,N-DIMETHYL-3-AMMONIO-1-PROPANESULFONATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；THE PROTEIN WAS CRYSTALLIZED BY THE HANGING DROP METHOD IN WHICH DROPS WERE COMPOSED OF VARIOUS RATIOS OF HIGF-I AT 7MG/ML (IN H2O) WITH RESERVOIR SOLUTION CONSISTING OF 0.1M TRIS.HCL PH 7.5, 12-15% (W/V) PEG 2K AND 5MM SB12 DETERGENT.
Resolution 2.54 Å R-free 0.265
1GZZ Human Insulin-like growth factor; Hamburg data Deposited 2002-06-10 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 49–118（70 aa）
Not recorded C15 N-DODECYL-N,N-DIMETHYL-3-AMMONIO-1-PROPANESULFONATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；THE PROTEIN WAS CRYSTALLIZED BY THE HANGING DROP METHOD IN WHICH DROPS WERE COMPOSED OF VARIOUS RATIOS OF HIGF-I AT 7MG/ML (IN H2O) WITH RESERVOIR SOLUTION CONSISTING OF 0.1M TRIS.HCL PH 7.5, 12-15% (W/V) PEG 2K AND 5MM SB12 DETERGENT.
Resolution 2.30 Å R-free 0.275
1H02 Human Insulin-like growth factor; SRS Daresbury data Deposited 2002-06-11 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 49–118（70 aa）
Not recorded C15 N-DODECYL-N,N-DIMETHYL-3-AMMONIO-1-PROPANESULFONATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；THE PROTEIN WAS CRYSTALLIZED BY THE HANGING DROP METHOD IN WHICH DROPS WERE COMPOSED OF VARIOUS RATIOS OF HIGF-I AT 7MG/ML (IN H2O) WITH RESERVOIR SOLUTION CONSISTING OF 0.1M TRIS.HCL PH 7.5, 12-15% (W/V) PEG 2K AND 5MM SB12 DETERGENT.
Resolution 2.00 Å R-free 0.300
1H59 Complex of IGFBP-5 with IGF-I Deposited 2001-05-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain A 49–118（70 aa） Fragment：RESIDUES 49-118
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.6；pH 5.60
Resolution 2.10 Å R-free 0.262
1IMX 1.8 Angstrom crystal structure of IGF-1 Deposited 2001-05-11 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 49–118（70 aa）
Not recorded BR BROMIDE ION × 1 CPQ N,N-BIS(3-D-GLUCONAMIDOPROPYL)DEOXYCHOLAMIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；PEG 3350, deoxy big CHAPS, sodium cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.82 Å R-free 0.258
2GF1 SOLUTION STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR 1: A NUCLEAR MAGNETIC RESONANCE AND RESTRAINED MOLECULAR DYNAMICS STUDY Deposited 1991-01-23 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 49–118（70 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
3GF1 SOLUTION STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR 1: A NUCLEAR MAGNETIC RESONANCE AND RESTRAINED MOLECULAR DYNAMICS STUDY Deposited 1991-01-24 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 49–118（70 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGF1A_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–29； UniProt 49–77 Author chain A； PDBConstruct 32–52； UniProt 90–110 Author chain B； PDBConstruct 1–29； UniProt 49–77 Author chain B； PDBConstruct 32–52； UniProt 90–110

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 1tgr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1tgr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1tgr
Deposition date deposition_date2004-05-29
Structure title titleCrystal Structure of mini-IGF-1(2)
Keywords keywordsIGF-I, IGF-1, Disulfide Isomerization, recepter binding, HORMONE-GROWTH FACTOR COMPLEX; HORMONE/GROWTH FACTOR
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier15.74 Å
Radius of gyration Rg (electron density) rg_electron14.45 Å
Forward intensity I(0) i03039610.00
Molecular weight molecular_weight11678.0 kDa
Excluded volume excluded_volume14407 ų
Envelope volume envelope_volume17691 ų
Hydration-shell volume shell_volume10862 ų
Envelope diameter envelope_diameter50.6 Å
Shell Rg shell_rg19.40 Å
Envelope Rg envelope_rg14.70 Å
Shape Rg shape_rg14.40 Å
Total Rg total_rg15.63 Å
Total atoms total_atoms810
Residues n_residues104
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 dmax52.3 Å
Rg (real space) rg_real15.69 Å
Rg uncertainty (real space) rg_real_error0.35 Å
I(0) (real space) i0_real3.0400e+06
I(0) uncertainty (real space) i0_real_error3.9470e+04
Rg (reciprocal space) rg_reciprocal15.70 Å
I(0) (reciprocal space) i0_reciprocal3040000.0000
Solution quality estimate total_estimate0.8878
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.9 Å
Skewness Skewness skewness0.205
Kurtosis Kurtosis kurtosis-0.265
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha247600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.850; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.990
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1tgra_
Class classg — Small proteins
Fold Fold foldg.1 — Insulin-like
Superfamily Superfamily superfamilyg.1.1 — Insulin-like
Family Family familyg.1.1.1 — Insulin-like
Domain ID domain_idd1tgrb_
Class classg — Small proteins
Fold Fold foldg.1 — Insulin-like
Superfamily Superfamily superfamilyg.1.1 — Insulin-like
Family Family familyg.1.1.1 — Insulin-like

CATH v4.4 (2 domains)

Domain ID domain_id1tgrA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology100 — Insulin-like, subunit E
Homologous superfamily homologous superfamily10 — Insulin-like
Domain ID domain_id1tgrB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology100 — Insulin-like, subunit E
Homologous superfamily homologous superfamily10 — Insulin-like
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8. Citations (1)

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9. Files and Curves (10)