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1oh2

Sucrose-Specific Porin, with Bound Sucrose Molecules

Method: X-RAY DIFFRACTION Dmax: 95.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Sucrose 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 Mutation：YES 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. 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 1OH2 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 mutation/modification 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
1A0T SUCROSE-SPECIFIC PORIN, WITH BOUND SUCROSE MOLECULES Deposited 1997-12-08 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）
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%. 2M SUCROSE WAS ADDED TO THE DROP FOR COCRYSTALLIZATION., vapor diffusion - sitting drop
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_SALTM
Isoform —
PDB entities 1, 2
Chains and sequence ranges Author chain P； PDBConstruct 1–413； UniProt 93–505 Author chain R； PDBConstruct 1–413； UniProt 93–505 Author chain Q； 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 1oh2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1oh2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1oh2
Deposition date deposition_date2003-05-21
Structure title titleSucrose-Specific Porin, with Bound Sucrose Molecules
Keywords keywordsMEMBRANE PROTEIN, OUTER MEMBRANE PROTEIN, TRANSPORT, SUGAR TRANSPORT, TRANSMEMBRANE; 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_guinier32.66 Å
Radius of gyration Rg (electron density) rg_electron31.88 Å
Forward intensity I(0) i0315726000.00
Molecular weight molecular_weight137610.0 kDa
Excluded volume excluded_volume169770 ų
Envelope volume envelope_volume211850 ų
Hydration-shell volume shell_volume52697 ų
Envelope diameter envelope_diameter94.1 Å
Shell Rg shell_rg40.99 Å
Envelope Rg envelope_rg31.42 Å
Shape Rg shape_rg31.88 Å
Total Rg total_rg32.55 Å
Total atoms total_atoms9717
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 dmax95.2 Å
Rg (real space) rg_real32.37 Å
Rg uncertainty (real space) rg_real_error0.42 Å
I(0) (real space) i0_real3.1570e+08
I(0) uncertainty (real space) i0_real_error4.0860e+06
Rg (reciprocal space) rg_reciprocal32.50 Å
I(0) (reciprocal space) i0_reciprocal315800000.0000
Solution quality estimate total_estimate0.8371
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary39.7 Å
Skewness Skewness skewness0.027
Kurtosis Kurtosis kurtosis-0.645
Angular range angular_range— – 0.2400 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35090000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.968; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; 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_idd1oh2p_
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_idd1oh2q_
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_idd1oh2r_
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_id1oh2P00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology170 — Maltoporin; Chain A
Homologous superfamily homologous superfamily10 — Porin, LamB type
Domain ID domain_id1oh2Q00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology170 — Maltoporin; Chain A
Homologous superfamily homologous superfamily10 — Porin, LamB type
Domain ID domain_id1oh2R00
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 (1)

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9. Files and Curves (10)