SAXSdb — 1fsb

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

P-SELECTIN

Homo sapiens

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 160–199	Fragment：EGF DOMAIN, RESIDUES 119 - 158	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 6；298 K	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 1FSB	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1G1Q Crystal structure of P-selectin lectin/EGF domains Deposited 2000-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 42–199（158 aa） Fragment：LECTIN/EGF DOMAINS Chain B 42–199（158 aa） Fragment：LECTIN/EGF DOMAINS Chain C 42–199（158 aa） Fragment：LECTIN/EGF DOMAINS Chain D 42–199（158 aa） Fragment：LECTIN/EGF DOMAINS	Not recorded	CA CALCIUM ION × 4 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；291 K；Tris-HCl, NaCl, CaCl2, 2-methyl-2,4-pentanediol, PEG 6000, pH 8.5, VAPOR DIFFUSION, HANGING DROP at 291K	Resolution 2.40 Å R-free 0.252
1G1R Crystal structure of P-selectin lectin/EGF domains complexed with SLeX Deposited 2000-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 42–199（158 aa） Fragment：LECTIN/EGF DOMAINS Chain B 42–199（158 aa） Fragment：LECTIN/EGF DOMAINS Chain C 42–199（158 aa） Fragment：LECTIN/EGF DOMAINS Chain D 42–199（158 aa） Fragment：LECTIN/EGF DOMAINS	Not recorded	CA CALCIUM ION × 4 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；291 K；Tris-HCl, NaCl, CaCl2, 2-methyl-2,4-pentanediol, PEG 6000, pH 8.5, VAPOR DIFFUSION, HANGING DROP at 291K	Resolution 3.40 Å R-free 0.322
1G1S P-SELECTIN LECTIN/EGF DOMAINS COMPLEXED WITH PSGL-1 PEPTIDE Deposited 2000-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 42–199（158 aa） Fragment：LECTIN/EGF DOMAINS Chain B 42–199（158 aa） Fragment：LECTIN/EGF DOMAINS	Not recorded	SR STRONTIUM ION × 2 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 7 NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；100 mM HEPES, 10 mM TRIS, 150 mN NaCl, 4 mM CaCl2, 50 mM SrCl2, 5% PEG 6000, 33% MPD, pH 7.0, VAPOR DIFFUSION, HANGING DROP at 291K	Resolution 1.90 Å R-free 0.235
1HES MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH P-selectin INTERNALIZATION PEPTIDE SHLGTYGVFTNAA Deposited 2000-11-24	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain P 813–830（18 aa） Fragment：INTERNALIZATION SIGNAL	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.1；289 K；HANGING DROP, 2.2M NACL, 0.4M NA/K PHOSPHATE, 10MM DTT 0.1M MES PH 7.1, 15% GLYCEROL, 16 DEGREES, MOLAR RATIO OF PEPTIDE TO PROTEIN 3:1	Resolution 3.00 Å R-free 0.266

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	LYAM3_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–40； UniProt 160–199

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	1fsb
Deposition date deposition_date	1996-03-25
Structure title title	STRUCTURE OF THE EGF DOMAIN OF P-SELECTIN, NMR, 19 STRUCTURES
Keywords keywords	EGF-LIKE DOMAIN, CELL ADHESION PROTEIN, TRANSMEMBRANE, GLYCOPROTEIN; CELL ADHESION PROTEIN
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	9.93 Å
Radius of gyration Rg (electron density) rg_electron	10.51 Å
Forward intensity I(0) i0	129287000.00
Molecular weight molecular_weight	84548.0 kDa
Excluded volume excluded_volume	100810 Å³
Envelope volume envelope_volume	10624 Å³
Hydration-shell volume shell_volume	8002 Å³
Envelope diameter envelope_diameter	45.2 Å
Shell Rg shell_rg	16.90 Å
Envelope Rg envelope_rg	12.74 Å
Shape Rg shape_rg	10.55 Å
Total Rg total_rg	10.56 Å
Total atoms total_atoms	5814
Residues n_residues	760
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	38.1 Å
Rg (real space) rg_real	10.06 Å
Rg uncertainty (real space) rg_real_error	0.50 Å
I(0) (real space) i0_real	1.2930e+08
I(0) uncertainty (real space) i0_real_error	1.4640e+06
Rg (reciprocal space) rg_reciprocal	10.05 Å
I(0) (reciprocal space) i0_reciprocal	129300000.0000
Solution quality estimate total_estimate	0.6968
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	35.7 Å
Skewness Skewness skewness	0.671
Kurtosis Kurtosis kurtosis	0.273
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	25870.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.554; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 0.408; 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_id	d1fsba_
Class class	g — Small proteins
Fold Fold fold	g.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamily	g.3.11 — EGF/Laminin
Family Family family	g.3.11.1 — EGF-type module

CATH v4.4 (1 domains)

Domain ID domain_id	1fsbA00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	25 — Laminin
Homologous superfamily homologous superfamily	10 — Laminin

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	P-SELECTIN
Molecular weight formula_weight	4455.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	5814

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606

STRUCTURE OF THE EGF DOMAIN OF P-SELECTIN, NMR, 19 STRUCTURES

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

P-SELECTIN

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/fs/1fsb/1fsb.fit
pddf	/app/data/pr_computation/fs/1fsb/1fsb.pr.out
profile	/app/data/saxs_computation/fs/1fsb/1fsb.dat