1c5a

THREE-DIMENSIONAL STRUCTURE OF PORCINE C5ADES*ARG FROM 1H NUCLEAR MAGNETIC RESONANCE DATA

Method: SOLUTION NMR D_max: 50.4 Å Quality: REASONABLE

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

COMPLEMENT C5A ANAPHYLATOXIN

Sus scrofa domestica

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 1–73	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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	CO5_PIG
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–73； UniProt 1–73

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1c5a
Deposition date deposition_date	1990-06-12
Structure title title	THREE-DIMENSIONAL STRUCTURE OF PORCINE C5ADES*ARG FROM 1H NUCLEAR MAGNETIC RESONANCE DATA
Keywords keywords	COMPLEMENT FACTOR; COMPLEMENT FACTOR
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	12.63 Å
Radius of gyration Rg (electron density) rg_electron	13.06 Å
Forward intensity I(0) i0	1450130000.00
Molecular weight molecular_weight	310610.0 kDa
Excluded volume excluded_volume	384090 Å³
Envelope volume envelope_volume	36006 Å³
Hydration-shell volume shell_volume	17668 Å³
Envelope diameter envelope_diameter	57.6 Å
Shell Rg shell_rg	23.36 Å
Envelope Rg envelope_rg	17.13 Å
Shape Rg shape_rg	13.05 Å
Total Rg total_rg	13.23 Å
Total atoms total_atoms	42968
Residues n_residues	2706
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	50.4 Å
Rg (real space) rg_real	12.64 Å
Rg uncertainty (real space) rg_real_error	0.44 Å
I(0) (real space) i0_real	1.4500e+09
I(0) uncertainty (real space) i0_real_error	1.5120e+07
Rg (reciprocal space) rg_reciprocal	12.64 Å
I(0) (reciprocal space) i0_reciprocal	1450000000.0000
Solution quality estimate total_estimate	0.6888
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	14.7 Å
Skewness Skewness skewness	0.451
Kurtosis Kurtosis kurtosis	-0.021
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1410000.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.449; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.604; 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	d1c5aa_
Class class	a — All alpha proteins
Fold Fold fold	a.50 — Anaphylotoxins (complement system)
Superfamily Superfamily superfamily	a.50.1 — Anaphylotoxins (complement system)
Family Family family	a.50.1.1 — Anaphylotoxins (complement system)

CATH v4.4 (1 domains)

Domain ID domain_id	1c5aA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	91 — Influenza Virus Matrix Protein; Chain A, domain 1
Homologous superfamily homologous superfamily	20 — Anaphylotoxins (complement system)

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8. Citations (2)

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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	COMPLEMENT C5A ANAPHYLATOXIN
Molecular weight formula_weight	8468.9 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	42968

来源生物 organism	Sus scrofa domestica
通用名 common_name	domestic pig
NCBI Class编号 ncbi_taxonomy_id	9825

THREE-DIMENSIONAL STRUCTURE OF PORCINE C5ADES*ARG FROM 1H NUCLEAR MAGNETIC RESONANCE DATA

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

COMPLEMENT C5A ANAPHYLATOXIN

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 (2)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/c5/1c5a/1c5a.fit
pddf	/app/data/pr_computation/c5/1c5a/1c5a.pr.out
profile	/app/data/saxs_computation/c5/1c5a/1c5a.dat