2ecs

Lambda Cro mutant Q27P/A29S/K32Q at 1.4 A in space group C2

Method: X-RAY DIFFRACTION Dmax: 59.9 Å Quality: GOOD

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

Phage lambda Cro

Enterobacteria phage lambda

UniProt P03040

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–66 Chain B; UniProt 1–66 Mutation:Q27P, A29S, K32Q SO4 SULFATE ION × 4 ACT ACETATE ION × 4 CL CHLORIDE ION × 1 LI LITHIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;298 K;80% saturated lithium sulfate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 1.40 Å R-free 0.175
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–66 Chain B; UniProt 1–66 Mutation:Q27P, A29S, K32Q SO4 SULFATE ION × 8 ACT ACETATE ION × 8 CL CHLORIDE ION × 2 LI LITHIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;298 K;80% saturated lithium sulfate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 1.40 Å R-free 0.175

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.

11 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RCRO_LAMBD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–66; UniProt 1–66 Author chain B; PDBConstruct 1–66; UniProt 1–66

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 2ecs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2ecs
Deposition date deposition_date2007-02-14
Structure title titleLambda Cro mutant Q27P/A29S/K32Q at 1.4 A in space group C2
Keywords keywordsTranscription factor, helix-turn-helix, bacteriophage, flexibility, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.28
Radius of gyration Rg (electron density) rg_electron17.20
Forward intensity I(0) i04014260.00
Molecular weight molecular_weight14049.0 kDa
Excluded volume excluded_volume17433 ų
Envelope volume envelope_volume21693 ų
Hydration-shell volume shell_volume11392 ų
Envelope diameter envelope_diameter59.8
Shell Rg shell_rg21.53
Envelope Rg envelope_rg17.26
Shape Rg shape_rg17.14
Total Rg total_rg18.18
Total atoms total_atoms981
Residues n_residues120
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 dmax59.9
Rg (real space) rg_real18.32
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real4.0140e+06
I(0) uncertainty (real space) i0_real_error4.5660e+04
Rg (reciprocal space) rg_reciprocal18.32
I(0) (reciprocal space) i0_reciprocal4014000.0000
Solution quality estimate total_estimate0.8669
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.0
Skewness Skewness skewness0.325
Kurtosis Kurtosis kurtosis-0.583
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha968200.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.792; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.940; Smooth: 0.948

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_idd2ecsa_
Class classa — All alpha proteins
Fold Fold folda.35 — lambda repressor-like DNA-binding domains
Superfamily Superfamily superfamilya.35.1 — lambda repressor-like DNA-binding domains
Family Family familya.35.1.2 — Phage repressors
Domain ID domain_idd2ecsb_
Class classa — All alpha proteins
Fold Fold folda.35 — lambda repressor-like DNA-binding domains
Superfamily Superfamily superfamilya.35.1 — lambda repressor-like DNA-binding domains
Family Family familya.35.1.2 — Phage repressors

CATH v4.4 (2 domains)

Domain ID domain_id2ecsA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology240 — CRO Repressor
Homologous superfamily homologous superfamily10 — CRO Repressor
Domain ID domain_id2ecsB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology240 — CRO Repressor
Homologous superfamily homologous superfamily10 — CRO Repressor

8. Citations (1)

9. Files and Curves (10)