SAXSdb — 1t2o

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

sortase

Staphylococcus aureus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9S446_STAAU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–146； UniProt 61–206 Author chain B； PDBConstruct 1–146； UniProt 61–206 Author chain C； PDBConstruct 1–146； UniProt 61–206

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	1t2o
Deposition date deposition_date	2004-04-22
Structure title title	Crystal structure of Se-SrtA, C184-Ala
Keywords keywords	Sortase, BETA BARREL, Transpeptidase, HYDROLASE; HYDROLASE
Experimental Method method	X-RAY DIFFRACTION

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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.

1t2o__assembly_1__model_1

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

Download this curve (.dat)

1t2o__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1t2o__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	15.67 Å
Rg (electron density)	14.42 Å
Total Rg	15.77 Å
Atom count	1133
Residues	141
Excluded volume	20298 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1t2o__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1t2o__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1t2o__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1t2oa_
Class class	b — All beta proteins
Fold Fold fold	b.100 — Sortase
Superfamily Superfamily superfamily	b.100.1 — Sortase
Family Family family	b.100.1.1 — Sortase

Domain ID domain_id	d1t2ob_
Class class	b — All beta proteins
Fold Fold fold	b.100 — Sortase
Superfamily Superfamily superfamily	b.100.1 — Sortase
Family Family family	b.100.1.1 — Sortase

Domain ID domain_id	d1t2oc_
Class class	b — All beta proteins
Fold Fold fold	b.100 — Sortase
Superfamily Superfamily superfamily	b.100.1 — Sortase
Family Family family	b.100.1.1 — Sortase

CATH v4.4 (3 domains)

Domain ID domain_id	1t2oA00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	260 — Sortase; Chain: A;
Homologous superfamily homologous superfamily	10 — Sortase

Domain ID domain_id	1t2oB00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	260 — Sortase; Chain: A;
Homologous superfamily homologous superfamily	10 — Sortase

Domain ID domain_id	1t2oC00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	260 — Sortase; Chain: A;
Homologous superfamily homologous superfamily	10 — Sortase

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Unit-cell length a length_a	46.553 Å
Unit-cell length b length_b	82.407 Å
Unit-cell length c length_c	56.112 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	104.17 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	17.710 Å
R factor r_factor	0.2210
R_work r_work	0.2210
R_free r_free	0.2750

Description description	sortase
Molecular weight formula_weight	16555.4 kDa
Mutation mutation	C184A
Source method src_method	man
Copy count entity_count	3

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	3425

Crystal structure of Se-SrtA, C184-Ala

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

sortase

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

1t2o__assembly_1__model_1

1t2o__assembly_1__model_1 | I(q)

1t2o__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (1)

Source organism organism	Staphylococcus aureus
NCBI taxonomy ID ncbi_taxonomy_id	1280
Host organism host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	53

Crystal structure of Se-SrtA, C184-Ala

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

sortase

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

1t2o__assembly_1__model_1

1t2o__assembly_1__model_1 | I(q)

1t2o__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (1)