SAXSdb — 3l2m

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

Pancreatic alpha-amylase

OrganismNot specified

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 Monomer Protein × 1 其他Polymer 3 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 16–511	Fragment：residues 16-511 Non-standard monomer：Yes (specific site not provided by mmCIF)	Cyclohexakis-(1-4)-(alpha-D-glucopyranose) × 3 CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；pH 6.75；298 K；0.010 M cacodylate, 0.002 M calcium chloride, soaking of alpha-cyclodextrin, pH 6.75, EVAPORATION, temperature 298K	Resolution 1.97 Å R-free 0.160

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 3L2M	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BVN PIG PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE PROTEINACEOUS INHIBITOR TENDAMISTAT Deposited 1998-09-16	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain P 1–496（496 aa）	Not recorded	CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；PROTEIN: 12 MG/ML IN 50 MM TRIS/HCL, PH 8.0, MIXED 5:1 WITH 40% (W/V) PEG 1000; RESERVOIR: 0.18-0.20 M SODIUM PHOSPHATE, PH 8.0 HARVESTED IN: 3 M SODIUM ACETATE, PH 7.5	Resolution 2.50 Å R-free 0.260
1DHK STRUCTURE OF PORCINE PANCREATIC ALPHA-AMYLASE Deposited 1996-10-14	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 2–496（495 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 6 CL CHLORIDE ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.85 Å R-free 0.220
1HX0 Structure of pig pancreatic alpha-amylase complexed with the "truncate" acarbose molecule (pseudotrisaccharide) Deposited 2001-01-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 16–511（496 aa）	Mutation：Q16PCA Non-standard monomer：Yes (specific site not provided by mmCIF)	CL CHLORIDE ION × 4 CA CALCIUM ION × 1 EDO 1,2-ETHANEDIOL × 12	X-RAY DIFFRACTION X-ray crystallization conditions batch；pH 8.5；277 K；CaCl2, pH 8.5, batch, temperature 277K	Resolution 1.38 Å R-free 0.130
1JFH STRUCTURE OF A PANCREATIC ALPHA-AMYLASE BOUND TO A SUBSTRATE ANALOGUE AT 2.03 ANGSTROM RESOLUTION Deposited 1997-09-19	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–496（495 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CL CHLORIDE ION × 1 HG MERCURY (II) ION × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.03 Å R-free 0.185
1KXQ Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase Deposited 2002-02-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–496（496 aa）	Not recorded	CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；Phosphate buffer 0.8 M, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.60 Å R-free 0.219
1KXQ Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase Deposited 2002-02-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–496（496 aa）	Not recorded	CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；Phosphate buffer 0.8 M, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.60 Å R-free 0.219
1KXQ Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase Deposited 2002-02-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–496（496 aa）	Not recorded	CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；Phosphate buffer 0.8 M, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.60 Å R-free 0.219
1KXQ Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase Deposited 2002-02-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–496（496 aa）	Not recorded	CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；Phosphate buffer 0.8 M, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.60 Å R-free 0.219
1KXT Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase Deposited 2002-02-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–496（496 aa）	Not recorded	CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；PEG 20000 15%, Malate imidazole 0.2M, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.236
1KXT Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase Deposited 2002-02-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–496（496 aa）	Not recorded	CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；PEG 20000 15%, Malate imidazole 0.2M, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.236
1KXT Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase Deposited 2002-02-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 1–496（496 aa）	Not recorded	CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；PEG 20000 15%, Malate imidazole 0.2M, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.236
1KXV Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase Deposited 2002-02-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–496（496 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；293 K；PEG4000 32%, Na citrate 0.1M & Ammonium Acetate 0.2M, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.60 Å R-free 0.229
1KXV Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase Deposited 2002-02-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–496（496 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；293 K；PEG4000 32%, Na citrate 0.1M & Ammonium Acetate 0.2M, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.60 Å R-free 0.229
1OSE Porcine pancreatic alpha-amylase complexed with acarbose Deposited 1996-03-20	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–496（495 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	BGC beta-D-glucopyranose × 1 CL CHLORIDE ION × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å R-free 0.222
1PIF PIG ALPHA-AMYLASE Deposited 1996-06-15	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 17–511（495 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；pH 6.0	Resolution 2.30 Å R-free 0.208
1PIG PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE OLIGOSACCHARIDE V-1532 Deposited 1996-06-15	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–496（495 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	HMC 5-HYDROXYMETHYL-CHONDURITOL × 1 BGC beta-D-glucopyranose × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6；VAPOR DIFFUSION; 10 MICROLITER OF PROTEIN (15 MG/ML IN 0.1 M AMMONIUM CACODYLATE, PH 10.0 0.001 M V-1532) WERE STEPWISE CONCENTRATED OVER 0.1, 0.15, AND 0.25 M AMMONIUM CACODYLATE, PH 6.0., vapor diffusion	Resolution 2.20 Å R-free 0.210
1PPI THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE. THE STRUCTURE OF THE COMPLEX OF A PANCREATIC ALPHA-AMYLASE WITH A CARBOHYDRATE INHIBITOR REFINED TO 2.2 ANGSTROMS RESOLUTION Deposited 1994-02-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–496（496 aa）	Not recorded	CL CHLORIDE ION × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å
1UA3 Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides Deposited 2003-02-27	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–496（496 aa）	Not recorded	CL CHLORIDE ION × 2 CA CALCIUM ION × 1 BGC beta-D-glucopyranose × 1 EDO 1,2-ETHANEDIOL × 6	X-RAY DIFFRACTION X-ray crystallization conditions LIQUID DIFFUSION；pH 8；277 K；Sodium chloride, Calsium chloride, pH 8.0, LIQUID DIFFUSION, temperature 277K	Resolution 2.01 Å R-free 0.196
1VAH Crystal structure of the pig pancreatic-amylase complexed with r-nitrophenyl-a-D-maltoside Deposited 2004-02-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 16–511（496 aa）	Not recorded	CL CHLORIDE ION × 1 CA CALCIUM ION × 1 NPO P-NITROPHENOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions LIQUID DIFFUSION；pH 8；295 K；SODIUM CHLORIDE, CALSIUM CHLORIDE, pH 8.0, LIQUID DIFFUSION, temperature 295K	Resolution 2.40 Å R-free 0.233
1WO2 Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion Deposited 2004-08-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 16–511（496 aa）	Mutation：Q16PCA Non-standard monomer：Yes (specific site not provided by mmCIF)	CL CHLORIDE ION × 1 CA CALCIUM ION × 1 EDO 1,2-ETHANEDIOL × 6	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 8；277 K；Tris, Calcium chloride, Sodium chloride, pH 8, EVAPORATION, temperature 277K	Resolution 2.01 Å R-free 0.184
3L2L X-ray Crystallographic Analysis of Pig Pancreatic Alpha-Amylase with Limit Dextrin and Oligosaccharide Deposited 2009-12-15	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 16–511（496 aa） Fragment：residues 16-511	Non-standard monomer：Yes (specific site not provided by mmCIF)	GLC alpha-D-glucopyranose × 1 CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6.75；298 K；0.010 M cacodylate, 0.002 M calcium chloride, pH 6.75, EVAPORATION, temperature 298K	Resolution 2.11 Å R-free 0.157
4X0N Porcine pancreatic alpha-amylase in complex with helianthamide, a novel proteinaceous inhibitor Deposited 2014-11-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 16–511（496 aa） Fragment：UNP residues 16-511	Non-standard monomer：Yes (specific site not provided by mmCIF)	CL CHLORIDE ION × 1 CA CALCIUM ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；300 K；100 mM Tris, 8% PEG 8000	Resolution 2.60 Å R-free 0.226

16 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	AMYP_PIG
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–496； UniProt 16–511

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3l2m
Deposition date deposition_date	2009-12-15
Structure title title	X-ray Crystallographic Analysis of Pig Pancreatic Alpha-Amylase with Alpha-cyclodextrin
Keywords keywords	;catalytic domain, carbohydrate binding module, alpha-cyclodextrin, Carbohydrate metabolism, Glycoprotein, Glycosidase, Metal-binding, Pyrrolidone carboxylic acid, Secreted, HYDROLASE ;; HYDROLASE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	24.43 Å
Radius of gyration Rg (electron density) rg_electron	23.38 Å
Forward intensity I(0) i0	59095700.00
Molecular weight molecular_weight	58392.0 kDa
Excluded volume excluded_volume	72181 Å³
Envelope volume envelope_volume	81878 Å³
Hydration-shell volume shell_volume	29018 Å³
Envelope diameter envelope_diameter	86.2 Å
Shell Rg shell_rg	31.07 Å
Envelope Rg envelope_rg	23.56 Å
Shape Rg shape_rg	23.34 Å
Total Rg total_rg	24.28 Å
Total atoms total_atoms	7975
Residues n_residues	495
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	83.0 Å
Rg (real space) rg_real	24.39 Å
Rg uncertainty (real space) rg_real_error	0.54 Å
I(0) (real space) i0_real	5.9100e+07
I(0) uncertainty (real space) i0_real_error	7.9540e+05
Rg (reciprocal space) rg_reciprocal	24.40 Å
I(0) (reciprocal space) i0_reciprocal	59100000.0000
Solution quality estimate total_estimate	0.8659
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	29.0 Å
Skewness Skewness skewness	0.384
Kurtosis Kurtosis kurtosis	-0.109
Angular range angular_range	— – 0.3250 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	12830000.0000
Real-space data points n_real_points	64
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.762; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.978

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Pancreatic alpha-amylase
Molecular weight formula_weight	55439.8 kDa
EC 编号 ec_number	3.2.1.1
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	9278

QYAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPPNENIVVTNPSRPWWERYQPVSYKLCTRSGNENEFRDMVTRCNNVGVRIYVDAVINHMCGSGAAAGTGTTCGSYCNPGNREFPAVPYSAWDFNDGKCKTASGGIESYNDPYQVRDCQLVGLLDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASKHMWPGDIKAVLDKLHNLNTNWFPAGSRPFIFQEVIDLGGEAIQSSEYFGNGRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKVAVGFMLAHPYGFTRVMSSYRWARNFVNGQDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWRQIRNMVWFRNVVDGQPFANWWDNGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYCDVISGDKVGNSCTGIKVYVSSDGTAQFSISNSAEDPFIAIHAESKL

Entity 2 Entity 2 branched

Description description	Cyclohexakis-(1-4)-(alpha-D-glucopyranose)
Molecular weight formula_weight	990.9 kDa
Source method src_method	man
Copy count entity_count	3

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	592

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d3l2ma1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.8 — (Trans)glycosidases
Family Family family	c.1.8.1 — Amylase, catalytic domain

Domain ID domain_id	d3l2ma2
Class class	b — All beta proteins
Fold Fold fold	b.71 — Glycosyl hydrolase domain
Superfamily Superfamily superfamily	b.71.1 — Glycosyl hydrolase domain
Family Family family	b.71.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id	3l2mA01
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	80 — Glycosidases

Domain ID domain_id	3l2mA02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	1180 — Golgi alpha-mannosidase II

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8. Citations (3)

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Unit-cell length a length_a	70.650 Å
Unit-cell length b length_b	114.880 Å
Unit-cell length c length_c	118.850 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.970 Å
Low-resolution limit resolution_low	29.300 Å
R factor r_factor	0.1300
R_work r_work	0.1267
R_free r_free	0.1602

fit	/app/data/saxs_computation/l2/3l2m/3l2m.fit
pddf	/app/data/pr_computation/l2/3l2m/3l2m.pr.out
profile	/app/data/saxs_computation/l2/3l2m/3l2m.dat

X-ray Crystallographic Analysis of Pig Pancreatic Alpha-Amylase with Alpha-cyclodextrin

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

Pancreatic alpha-amylase

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction