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1a0t

SUCROSE-SPECIFIC PORIN, WITH BOUND SUCROSE MOLECULES

Method: X-RAY DIFFRACTION Dmax: 93.7 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

SUCROSE-SPECIFIC PORIN

Salmonella typhimurium

UniProt P22340

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 6 PDB declaration: trimeric（3） Consistent with protein copy count Chain P； UniProt 93–505 Chain Q； UniProt 93–505 Chain R； UniProt 93–505 Not recorded beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose × 6 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.7；PROTEIN WAS CRYSTALLIZED BY VAPOR DIFFUSION USING THE SITTING-DROP METHOD. THE DROP CONTAINED 5-7 MG/ML PROTEIN, 20 MM TRIS/CL AT PH 7.7, 100MM LICL, 20MM MGSO4, 1.2% BETA-D-OCTYLGLUCOPYRANOSIDE AND 6-9% PEG-2000. THE CONCENTRATION OF PEG IN THE RESERVOIR WAS 12-15%. 2M SUCROSE WAS ADDED TO THE DROP FOR COCRYSTALLIZATION., vapor diffusion - sitting drop Resolution 2.40 Å R-free 0.246

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 1A0T Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1A0S SUCROSE-SPECIFIC PORIN Deposited 1997-12-07 Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain P 93–505（413 aa）
Chain Q 93–505（413 aa）
Chain R 93–505（413 aa）
Not recorded CA CALCIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.7；PROTEIN WAS CRYSTALLIZED BY VAPOR DIFFUSION USING THE SITTING-DROP METHOD. THE DROP CONTAINED 5-7 MG/ML PROTEIN, 20 MM TRIS/CL AT PH 7.7, 100MM LICL, 20MM MGSO4, 1.2% BETA-D-OCTYLGLUCOPYRANOSIDE AND 6-9% PEG-2000. THE CONCENTRATION OF PEG IN THE RESERVOIR WAS 12-15%., vapor diffusion - sitting drop
Resolution 2.40 Å R-free 0.228
1OH2 Sucrose-Specific Porin, with Bound Sucrose Molecules Deposited 2003-05-21 Different mutation/modification Different experimental conditions Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric
Chain P 93–505（413 aa）
Chain Q 93–505（413 aa）
Chain R 93–505（413 aa）
Mutation：YES CA CALCIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.7；PROTEIN WAS CRYSTALLIZED BY VAPOR DIFFUSION USING THE SITTING-DROP METHOD. THE DROP CONTAINED 5-7 MG/ML PROTEIN, 20 MM TRIS/CL AT PH 7.7, 100MM LICL, 20MM MGSO4, 1.2% BETA-D-OCTYLGLUCOPYRANOSIDE AND 6-9% PEG-2000. THE CONCENTRATION OF PEG IN THE RESERVOIR WAS 12-15%. 2M SUCROSE WAS ADDED TO THE DROP FOR COCRYSTALLIZATION.
Resolution 2.40 Å R-free 0.246

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

View Construct and Data Evidence
UniProt name SCRY_SALTY
Isoform —
PDB entities 1
Chains and sequence ranges Author chain P； PDBConstruct 1–413； UniProt 93–505 Author chain Q； PDBConstruct 1–413； UniProt 93–505 Author chain R； PDBConstruct 1–413； UniProt 93–505

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 1a0t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a0t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a0t
Deposition date deposition_date1997-12-08
Structure title titleSUCROSE-SPECIFIC PORIN, WITH BOUND SUCROSE MOLECULES
Keywords keywordsOUTER MEMBRANE PROTEIN, PORIN; OUTER MEMBRANE PROTEIN
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_guinier32.60 Å
Radius of gyration Rg (electron density) rg_electron31.85 Å
Forward intensity I(0) i0319302000.00
Molecular weight molecular_weight138020.0 kDa
Excluded volume excluded_volume170080 ų
Envelope volume envelope_volume211820 ų
Hydration-shell volume shell_volume52701 ų
Envelope diameter envelope_diameter94.1 Å
Shell Rg shell_rg41.02 Å
Envelope Rg envelope_rg31.41 Å
Shape Rg shape_rg31.86 Å
Total Rg total_rg32.53 Å
Total atoms total_atoms9747
Residues n_residues1239
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 dmax93.7 Å
Rg (real space) rg_real32.31 Å
Rg uncertainty (real space) rg_real_error0.39 Å
I(0) (real space) i0_real3.1930e+08
I(0) uncertainty (real space) i0_real_error4.3040e+06
Rg (reciprocal space) rg_reciprocal32.44 Å
I(0) (reciprocal space) i0_reciprocal319300000.0000
Solution quality estimate total_estimate0.8399
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.2 Å
Skewness Skewness skewness0.031
Kurtosis Kurtosis kurtosis-0.643
Angular range angular_range— – 0.2450 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36200000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.978; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1a0tp_
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_idd1a0tq_
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_idd1a0tr_
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_id1a0tP00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology170 — Maltoporin; Chain A
Homologous superfamily homologous superfamily10 — Porin, LamB type
Domain ID domain_id1a0tQ00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology170 — Maltoporin; Chain A
Homologous superfamily homologous superfamily10 — Porin, LamB type
Domain ID domain_id1a0tR00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology170 — Maltoporin; Chain A
Homologous superfamily homologous superfamily10 — Porin, LamB type
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8. Citations (2)

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9. Files and Curves (10)