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1tki

AUTOINHIBITED SERINE KINASE DOMAIN OF THE GIANT MUSCLE PROTEIN TITIN

Method: X-RAY DIFFRACTION Dmax: 142.9 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

TITIN

Homo sapiens

UniProt Q10466

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 24748–25068 Fragment：KINASE No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 Å R-free 0.248
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 24748–25068 Fragment：KINASE No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 Å R-free 0.248

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 1TKI Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BPV TITIN MODULE A71 FROM HUMAN CARDIAC MUSCLE, NMR, 50 STRUCTURES Deposited 1998-08-11 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 14859–14961（103 aa） Fragment：71 TH DOMAIN FROM THE A-BAND
Mutation：I9V No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.6；310 K；Ionic strength (raw mmCIF value) 50 mM NACL
NMR sample composition 10 MM ACETATE BUFFER
Resolution not provided
1G1C I1 DOMAIN FROM TITIN Deposited 2000-10-11 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2027–2125（99 aa） Fragment：MOST N-TERMINAL IG DOMAIN, RESIDUES 2027-2125
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；294 K；3.25 M NaCl, 0.1 M Tris-HCL pH 8.0, 1mM EDTA, 1mM DTT, pH 8.0, VAPOR DIFFUSION, HANGING DROP at 294K
Resolution 2.10 Å R-free 0.248
1G1C I1 DOMAIN FROM TITIN Deposited 2000-10-11 Different construct Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 2027–2125（99 aa） Fragment：MOST N-TERMINAL IG DOMAIN, RESIDUES 2027-2125
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；294 K；3.25 M NaCl, 0.1 M Tris-HCL pH 8.0, 1mM EDTA, 1mM DTT, pH 8.0, VAPOR DIFFUSION, HANGING DROP at 294K
Resolution 2.10 Å R-free 0.248
1NCT TITIN MODULE M5, N-TERMINALLY EXTENDED, NMR Deposited 1996-08-13 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 26059–26155（97 aa） Fragment：N-TERMINALLY EXTENDED MODULE M5
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.8；300 K
Resolution not provided
1NCU Titin Module M5, N-terminally Extended, NMR Deposited 1996-08-13 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 26059–26155（97 aa） Fragment：N-TERMINALLY EXTENDED MODULE M5
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.8；300 K
Resolution not provided
1TIT TITIN, IG REPEAT 27, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1996-02-02 Different construct Different experimental method Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 5253–5341（89 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1TIU TITIN, IG REPEAT 27, NMR, 24 STRUCTURES Deposited 1996-02-02 Different construct Different experimental method Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 5253–5341（89 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided

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

View Construct and Data Evidence
UniProt name Q10466_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–321； UniProt 24748–25068 Author chain B； PDBConstruct 1–321； UniProt 24748–25068

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 1tki

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1tki
Deposition date deposition_date1998-05-29
Structure title titleAUTOINHIBITED SERINE KINASE DOMAIN OF THE GIANT MUSCLE PROTEIN TITIN
Keywords keywordsSERINE KINASE, TITIN, MUSCLE, AUTOINHIBITION; SERINE KINASE
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_guinier46.79 Å
Radius of gyration Rg (electron density) rg_electron47.15 Å
Forward intensity I(0) i076732300.00
Molecular weight molecular_weight74196.0 kDa
Excluded volume excluded_volume93643 ų
Envelope volume envelope_volume139710 ų
Hydration-shell volume shell_volume24416 ų
Envelope diameter envelope_diameter145.0 Å
Shell Rg shell_rg53.81 Å
Envelope Rg envelope_rg44.53 Å
Shape Rg shape_rg47.10 Å
Total Rg total_rg47.61 Å
Total atoms total_atoms5224
Residues n_residues642
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 dmax142.9 Å
Rg (real space) rg_real47.39 Å
Rg uncertainty (real space) rg_real_error1.37 Å
I(0) (real space) i0_real7.6730e+07
I(0) uncertainty (real space) i0_real_error1.5340e+06
Rg (reciprocal space) rg_reciprocal46.80 Å
I(0) (reciprocal space) i0_reciprocal76670000.0000
Solution quality estimate total_estimate0.5512
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.2 Å
Skewness Skewness skewness0.188
Kurtosis Kurtosis kurtosis-1.395
Angular range angular_range— – 0.1700 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6744000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.005; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.069; Smooth: 0.077
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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) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1tkia_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.7 — Protein kinases, catalytic subunit
Domain ID domain_idd1tkib_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.7 — Protein kinases, catalytic subunit

CATH v4.4 (4 domains)

Domain ID domain_id1tkiA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id1tkiA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id1tkiB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id1tkiB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
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8. Citations (2)

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9. Files and Curves (10)