3p71

Crystal structure of the complex of LCMT-1 and PP2A

Method: X-RAY DIFFRACTION Dmax: 92.8 Å Quality: GOOD

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

Leucine carboxyl methyltransferase 1

Homo sapiens

UniProt Q9UIC8

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain T; UniProt 1–334 Mutation:C19M, A21E, D22N, P115S Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) PEG DI(HYDROXYETHYL)ETHER × 1 AN6 5'-{[(3S)-3-amino-3-carboxypropyl](ethyl)amino}-5'-deoxyadenosine × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.2;291 K;PROTEIN COMPLEX (~5 MG/ML), 100MM TRIS-HCL, 22-26% V/V PEG 4000, 200 MM SODIUM ACETATE, 5 MM DTT, pH 8.2, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 2.70 Å R-free 0.249

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.

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

View Construct and Data Evidence
UniProt name LCMT1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain T; PDBConstruct 1–334; UniProt 1–334

Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform

Homo sapiens

UniProt P67775

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–309 Fragment:CATALYTIC SUBUNIT ALPHA ISOFORM Leucine carboxyl methyltransferase 1 × 1 (Q9UIC8) PEG DI(HYDROXYETHYL)ETHER × 1 AN6 5'-{[(3S)-3-amino-3-carboxypropyl](ethyl)amino}-5'-deoxyadenosine × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.2;291 K;PROTEIN COMPLEX (~5 MG/ML), 100MM TRIS-HCL, 22-26% V/V PEG 4000, 200 MM SODIUM ACETATE, 5 MM DTT, pH 8.2, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 2.70 Å R-free 0.249

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.

49 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PP2AA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–304; UniProt 1–309

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 3p71

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3p71
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3p71
Deposition date deposition_date2010-10-11
Structure title titleCrystal structure of the complex of LCMT-1 and PP2A
Keywords keywords;LEUCINE CARBOXYMETHYLTRANSFERASE-1, SERINE/THREONINE PROTEIN KEYWDS 2 PHOSPHATASE 2A, METHYLTRANSFERASE, S-ADENOSYL-L-METHIONINE, TRANSFERASE-HYDROLASE complex ;; TRANSFERASE/HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.35
Radius of gyration Rg (electron density) rg_electron27.81
Forward intensity I(0) i086363900.00
Molecular weight molecular_weight71864.0 kDa
Excluded volume excluded_volume89338 ų
Envelope volume envelope_volume106140 ų
Hydration-shell volume shell_volume32290 ų
Envelope diameter envelope_diameter99.2
Shell Rg shell_rg34.78
Envelope Rg envelope_rg28.02
Shape Rg shape_rg27.81
Total Rg total_rg28.47
Total atoms total_atoms5039
Residues n_residues618
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 dmax92.8
Rg (real space) rg_real28.47
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real8.6360e+07
I(0) uncertainty (real space) i0_real_error1.3060e+06
Rg (reciprocal space) rg_reciprocal28.44
I(0) (reciprocal space) i0_reciprocal86360000.0000
Solution quality estimate total_estimate0.8733
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary91.2
Skewness Skewness skewness0.452
Kurtosis Kurtosis kurtosis-0.404
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha39000000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.820; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.949; Smooth: 0.940

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3p71c_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.159 — Metallo-dependent phosphatases
Superfamily Superfamily superfamilyd.159.1 — Metallo-dependent phosphatases
Family Family familyd.159.1.3 — Protein serine/threonine phosphatase
Domain ID domain_idd3p71t_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.66 — S-adenosyl-L-methionine-dependent methyltransferases
Superfamily Superfamily superfamilyc.66.1 — S-adenosyl-L-methionine-dependent methyltransferases
Family Family familyc.66.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id3p71C00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology21 — Purple Acid Phosphatase; chain A, domain 2
Homologous superfamily homologous superfamily10 — Metallo-dependent phosphatases
Domain ID domain_id3p71T00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily150 — Vaccinia Virus protein VP39

8. Citations (1)

9. Files and Curves (10)