1af6

MALTOPORIN SUCROSE COMPLEX

Method: X-RAY DIFFRACTION Dmax: 98.1 Å Quality: EXCELLENT

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

MALTOPORIN

Escherichia coli

UniProt P02943

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Homooligomer Protein × 3 其他Polymer 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 26–446 Chain B; UniProt 26–446 Chain C; UniProt 26–446 Not recorded beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose × 3 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;pH 7. Resolution 2.40 Å R-free 0.214

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LAMB_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–421; UniProt 26–446 Author chain B; PDBConstruct 1–421; UniProt 26–446 Author chain C; PDBConstruct 1–421; UniProt 26–446

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 1af6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1af6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1af6
Deposition date deposition_date1997-03-21
Structure title titleMALTOPORIN SUCROSE COMPLEX
Keywords keywordsMEMBRANE PROTEIN, SPECIFIC PORIN, BETA BARREL, SUGAR TRANSPORT, SUCROSE; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.50
Radius of gyration Rg (electron density) rg_electron32.75
Forward intensity I(0) i0344772000.00
Molecular weight molecular_weight143230.0 kDa
Excluded volume excluded_volume176070 ų
Envelope volume envelope_volume228430 ų
Hydration-shell volume shell_volume55336 ų
Envelope diameter envelope_diameter97.0
Shell Rg shell_rg42.09
Envelope Rg envelope_rg32.05
Shape Rg shape_rg32.74
Total Rg total_rg33.46
Total atoms total_atoms10123
Residues n_residues1263
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 dmax98.1
Rg (real space) rg_real33.26
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real3.4480e+08
I(0) uncertainty (real space) i0_real_error5.6130e+06
Rg (reciprocal space) rg_reciprocal33.41
I(0) (reciprocal space) i0_reciprocal344800000.0000
Solution quality estimate total_estimate0.9070
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.8
Skewness Skewness skewness-0.035
Kurtosis Kurtosis kurtosis-0.669
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26160000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.955; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.966; Smooth: 0.961

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1af6a_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.4 — Transmembrane beta-barrels
Superfamily Superfamily superfamilyf.4.3 — Porins
Family Family familyf.4.3.2 — Maltoporin-like
Domain ID domain_idd1af6b_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.4 — Transmembrane beta-barrels
Superfamily Superfamily superfamilyf.4.3 — Porins
Family Family familyf.4.3.2 — Maltoporin-like
Domain ID domain_idd1af6c_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.4 — Transmembrane beta-barrels
Superfamily Superfamily superfamilyf.4.3 — Porins
Family Family familyf.4.3.2 — Maltoporin-like

CATH v4.4 (3 domains)

Domain ID domain_id1af6A00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology170 — Maltoporin; Chain A
Homologous superfamily homologous superfamily10 — Porin, LamB type
Domain ID domain_id1af6B00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology170 — Maltoporin; Chain A
Homologous superfamily homologous superfamily10 — Porin, LamB type
Domain ID domain_id1af6C00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology170 — Maltoporin; Chain A
Homologous superfamily homologous superfamily10 — Porin, LamB type

8. Citations (3)

9. Files and Curves (10)