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1bip

BIFUNCTIONAL PROTEINASE INHIBITOR TRYPSIN/A-AMYLASE FROM SEEDS OF RAGI (ELEUSINE CORACANA GAERTNERI)

Method: SOLUTION NMR Dmax: 53.8 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ALPHA-AMYLASE/TRYPSIN INHIBITOR

Eleusine coracana

UniProt P01087

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–122 Not recorded No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions Resolution not provided

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 1BIP Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1B1U CRYSTAL STRUCTURE OF THE BIFUNCTIONAL INHIBITOR RAGI Deposited 1998-11-23 Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–122（122 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；1.15M AMMONIUM SULFATE, 0.2M AMMONIUM PHOSPHATE PH 8.0
Resolution 2.20 Å R-free 0.321
1TMQ STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR Deposited 1998-01-13 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–117（117 aa）
Not recorded CL CHLORIDE ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions 200MM AMMONIUM PHOSPHATE, 100MM TRIS-HCL, PH 8.5, 50% (W/V) 2-METHYL-2,4- PENTANEDIOL
Resolution 2.50 Å R-free 0.261

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

View Construct and Data Evidence
UniProt name IAAT_ELECO
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–122； UniProt 1–122

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 1bip

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bip
Deposition date deposition_date1995-03-31
Structure title titleBIFUNCTIONAL PROTEINASE INHIBITOR TRYPSIN/A-AMYLASE FROM SEEDS OF RAGI (ELEUSINE CORACANA GAERTNERI)
Keywords keywordsSERINE PROTEINASE INHIBITOR; SERINE PROTEINASE INHIBITOR
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier14.98 Å
Radius of gyration Rg (electron density) rg_electron14.75 Å
Forward intensity I(0) i01070390000.00
Molecular weight molecular_weight262610.0 kDa
Excluded volume excluded_volume323460 ų
Envelope volume envelope_volume38950 ų
Hydration-shell volume shell_volume18033 ų
Envelope diameter envelope_diameter61.5 Å
Shell Rg shell_rg24.58 Å
Envelope Rg envelope_rg18.73 Å
Shape Rg shape_rg14.76 Å
Total Rg total_rg14.90 Å
Total atoms total_atoms36360
Residues n_residues2440
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 dmax53.8 Å
Rg (real space) rg_real14.92 Å
Rg uncertainty (real space) rg_real_error0.41 Å
I(0) (real space) i0_real1.0700e+09
I(0) uncertainty (real space) i0_real_error1.2730e+07
Rg (reciprocal space) rg_reciprocal14.92 Å
I(0) (reciprocal space) i0_reciprocal1070000000.0000
Solution quality estimate total_estimate0.5899
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary19.1 Å
Skewness Skewness skewness0.216
Kurtosis Kurtosis kurtosis-0.190
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha364200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.650; Stabil: 1.000; Sysdev: 0.256; Positv: 1.000; Valcen: 0.947; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bipa_
Class classa — All alpha proteins
Fold Fold folda.52 — Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin
Superfamily Superfamily superfamilya.52.1 — Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin
Family Family familya.52.1.2 — Proteinase/alpha-amylase inhibitors

CATH v4.4 (1 domains)

Domain ID domain_id1bipA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology110 — Hydrophobic Seed Protein
Homologous superfamily homologous superfamily10 — Plant lipid-transfer and hydrophobic proteins
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8. Citations (1)

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9. Files and Curves (10)