SAXSdb — 1hcx

▼

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

MAJOR AUTOLYSIN

STREPTOCOCCUS PNEUMONIAE

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	;2,2':6',2''-TERPYRIDINE PLATINUM(II) Chloride ; × 1 CHOLINE ION × 5 DECYLAMINE-N,N-DIMETHYL-N-OXIDE × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ALYS_STRPN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–127； UniProt 192–318 Author chain B； PDBConstruct 1–127； UniProt 192–318

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1hcx
Deposition date deposition_date	2001-05-10
Structure title title	Choline binding domain of the major autolysin (C-LytA) from Streptococcus pneumoniae
Keywords keywords	CHOLINE-BINDING DOMAIN, CELL WALL ATTACHMENT; CHOLINE-BINDING DOMAIN
Experimental Method method	X-RAY DIFFRACTION

▼

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1hcx__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1hcx__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1hcx__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	26.42 Å
Rg (electron density)	25.63 Å
Total Rg	26.43 Å
Atom count	2204
Residues	254
Excluded volume	39297 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1hcx__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	MAJOR AUTOLYSIN
Molecular weight formula_weight	14949.6 kDa
EC 编号 ec_number	3.5.1.28
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	2283

GSYPKDKFEKINGTWYYFDSSGYMLADRWRKHTDGNWYWFDNSGEMATGWKKIADKWYYFNEEGAMKTGWVKYKDTWYYLDAKEGAMVSNAFIQSADGTGWYYLKPDGTLADRPEFTVEPDGLITVK

Source Source

Source organism organism	STREPTOCOCCUS PNEUMONIAE
NCBI taxonomy ID ncbi_taxonomy_id	1313
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	;2,2':6',2''-TERPYRIDINE PLATINUM(II) Chloride ;
Molecular weight formula_weight	463.8 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	CHOLINE ION
Molecular weight formula_weight	104.2 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 4 Entity 4 non-polymer

Description description	DECYLAMINE-N,N-DIMETHYL-N-OXIDE
Molecular weight formula_weight	201.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	79

▼

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1hcxa_
Class class	b — All beta proteins
Fold Fold fold	b.109 — beta-hairpin stack
Superfamily Superfamily superfamily	b.109.1 — Cell wall binding repeat
Family Family family	b.109.1.1 — Cell wall binding repeat

Domain ID domain_id	d1hcxb_
Class class	b — All beta proteins
Fold Fold fold	b.109 — beta-hairpin stack
Superfamily Superfamily superfamily	b.109.1 — Cell wall binding repeat
Family Family family	b.109.1.1 — Cell wall binding repeat

CATH v4.4 (2 domains)

Domain ID domain_id	1hcxA00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	270 — left handed beta-beta-3-solenoid
Homologous superfamily homologous superfamily	10 — Cholin Binding

Domain ID domain_id	1hcxB00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	270 — left handed beta-beta-3-solenoid
Homologous superfamily homologous superfamily	10 — Cholin Binding

▶

Unit-cell length a length_a	58.049 Å
Unit-cell length b length_b	118.177 Å
Unit-cell length c length_c	104.859 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	16

Space group space_group	I 2 2 2
Space-group number int_tables_number	23
Crystal system crystal_system	—

Resolution resolution	2.600 Å
Low-resolution limit resolution_low	34.900 Å
R factor r_factor	0.2390
R_work r_work	0.2390
R_free r_free	0.3020

Choline binding domain of the major autolysin (C-LytA) from Streptococcus pneumoniae

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

MAJOR AUTOLYSIN

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1hcx__assembly_1__model_1

1hcx__assembly_1__model_1 | I(q)

1hcx__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (2)

Choline binding domain of the major autolysin (C-LytA) from Streptococcus pneumoniae

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

MAJOR AUTOLYSIN

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1hcx__assembly_1__model_1

1hcx__assembly_1__model_1 | I(q)

1hcx__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (2)