5w0z

Crystal structure of MBP fused activation-induced cytidine deaminase (AID)

Method: X-RAY DIFFRACTION Dmax: 163.6 Å Quality: REASONABLE

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

MBP fused activation-induced cytidine deaminase

Homo sapiens

UniProt P0AEY0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 27–392 Fragment:UNP P0AEY0 residues 27-392,UNP Q9GZX7 residues 13-181 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;0.26 M NaCl, 0.1 M MES pH 6.0, 12% PEG3350 Resolution 3.61 Å R-free 0.307
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 27–392 Fragment:UNP P0AEY0 residues 27-392,UNP Q9GZX7 residues 13-181 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;0.26 M NaCl, 0.1 M MES pH 6.0, 12% PEG3350 Resolution 3.61 Å R-free 0.307

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.

109 other PDB entries and 147 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECO57
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–367; UniProt 27–392 Author chain B; PDBConstruct 2–367; UniProt 27–392

MBP fused activation-induced cytidine deaminase

Homo sapiens

UniProt Q9GZX7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 13–181 Fragment:UNP P0AEY0 residues 27-392,UNP Q9GZX7 residues 13-181 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;0.26 M NaCl, 0.1 M MES pH 6.0, 12% PEG3350 Resolution 3.61 Å R-free 0.307
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 13–181 Fragment:UNP P0AEY0 residues 27-392,UNP Q9GZX7 residues 13-181 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;0.26 M NaCl, 0.1 M MES pH 6.0, 12% PEG3350 Resolution 3.61 Å R-free 0.307

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.

4 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AICDA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 381–549; UniProt 13–181 Author chain B; PDBConstruct 381–549; UniProt 13–181

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 5w0z

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5w0z
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5w0z
Deposition date deposition_date2017-06-01
Structure title titleCrystal structure of MBP fused activation-induced cytidine deaminase (AID)
Keywords keywordsClass switch recombination, Cytidine deaminase, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier55.83
Radius of gyration Rg (electron density) rg_electron56.03
Forward intensity I(0) i0198741000.00
Molecular weight molecular_weight120830.0 kDa
Excluded volume excluded_volume152120 ų
Envelope volume envelope_volume242510 ų
Hydration-shell volume shell_volume35975 ų
Envelope diameter envelope_diameter180.9
Shell Rg shell_rg60.69
Envelope Rg envelope_rg52.89
Shape Rg shape_rg56.01
Total Rg total_rg56.27
Total atoms total_atoms8536
Residues n_residues1076
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 dmax163.6
Rg (real space) rg_real56.27
Rg uncertainty (real space) rg_real_error1.80
I(0) (real space) i0_real1.9870e+08
I(0) uncertainty (real space) i0_real_error3.8420e+06
Rg (reciprocal space) rg_reciprocal55.38
I(0) (reciprocal space) i0_reciprocal198500000.0000
Solution quality estimate total_estimate0.6349
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary29.2
Skewness Skewness skewness0.211
Kurtosis Kurtosis kurtosis-1.179
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6617000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.308; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.328; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5w0zA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology140 — Cytidine Deaminase; domain 2
Homologous superfamily homologous superfamily10 — Cytidine Deaminase, domain 2
Domain ID domain_id5w0zB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology140 — Cytidine Deaminase; domain 2
Homologous superfamily homologous superfamily10 — Cytidine Deaminase, domain 2

8. Citations (1)

9. Files and Curves (10)