1mpo

MALTOPORIN MALTOHEXAOSE COMPLEX

Method: X-RAY DIFFRACTION Dmax: 93.5 Å Quality: REASONABLE

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

MALTOPORIN

OrganismNot specified

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 ;alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose ; × 3 MG MAGNESIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;pH 7. Resolution 2.80 Å R-free 0.251

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 1mpo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1mpo
Deposition date deposition_date1996-01-11
Structure title titleMALTOPORIN MALTOHEXAOSE COMPLEX
Keywords keywordsMEMBRANE PROTEIN, SPECIFIC PORIN, BETA BARREL MEMBRANE PROTEIN, SUGAR TRANSPORT, BETA BARREL; 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) i0351347000.00
Molecular weight molecular_weight144670.0 kDa
Excluded volume excluded_volume177850 ų
Envelope volume envelope_volume228640 ų
Hydration-shell volume shell_volume55418 ų
Envelope diameter envelope_diameter96.1
Shell Rg shell_rg42.07
Envelope Rg envelope_rg32.03
Shape Rg shape_rg32.74
Total Rg total_rg33.43
Total atoms total_atoms10221
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 dmax93.5
Rg (real space) rg_real33.18
Rg uncertainty (real space) rg_real_error0.14
I(0) (real space) i0_real3.3830e+08
I(0) uncertainty (real space) i0_real_error3.7890e+06
Rg (reciprocal space) rg_reciprocal33.41
I(0) (reciprocal space) i0_reciprocal351400000.0000
Solution quality estimate total_estimate0.7267
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.8
Skewness Skewness skewness-0.037
Kurtosis Kurtosis kurtosis-0.677
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha4.7710
Highest regularization parameter α highest_alpha27150000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.988; Stabil: 0.910; Sysdev: 0.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.792

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_idd1mpoa_
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_idd1mpob_
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_idd1mpoc_
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_id1mpoA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology170 — Maltoporin; Chain A
Homologous superfamily homologous superfamily10 — Porin, LamB type
Domain ID domain_id1mpoB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology170 — Maltoporin; Chain A
Homologous superfamily homologous superfamily10 — Porin, LamB type
Domain ID domain_id1mpoC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology170 — Maltoporin; Chain A
Homologous superfamily homologous superfamily10 — Porin, LamB type

8. Citations (2)

9. Files and Curves (10)