SAXSdb — 3r90

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

Malignant T cell-amplified sequence 1

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 12	SULFATE ION × 25 UNKNOWN ATOM OR ION × 174 GLYCEROL × 1 water × 12	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MCTS1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–181； UniProt 1–181 Author chain B； PDBConstruct 1–181； UniProt 1–181 Author chain C； PDBConstruct 1–181； UniProt 1–181 Author chain D； PDBConstruct 1–181； UniProt 1–181 Author chain E； PDBConstruct 1–181； UniProt 1–181 Author chain F； PDBConstruct 1–181； UniProt 1–181 Author chain G； PDBConstruct 1–181； UniProt 1–181 Author chain H； PDBConstruct 1–181； UniProt 1–181 Author chain I； PDBConstruct 1–181； UniProt 1–181 Author chain J； PDBConstruct 1–181； UniProt 1–181 Author chain K； PDBConstruct 1–181； UniProt 1–181 Author chain L； PDBConstruct 1–181； UniProt 1–181

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	3r90
Deposition date deposition_date	2011-03-24
Structure title title	Crystal structure of Malignant T cell-amplified sequence 1 protein
Keywords keywords	structural genomics consortium, surface entropy reduction, SGC, RNA binding Protein; RNA BINDING PROTEIN
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.

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3r90__assembly_1__model_1`	dodecameric （12）	Excluded	—	—
	Exclusion reason： The source record does not identify the atom or ion element unambiguously, so a reliable calculation is not possible.

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Malignant T cell-amplified sequence 1
Molecular weight formula_weight	21312.1 kDa
Mutation mutation	E137A, K139A, Q140A
Source method src_method	man
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L
Atom count atom_count	19275

MFKKFDEKENVSNCIQLKTSVIKGIKNQLIEQFPGIEPWLNQIMPKKDPVKIVRCHEHIEILTVNGELLFFRQREGPFYPTLRLLHKYPFILPHQQVDKGAIKFVLSGANIMCPGLTSPGAKLYPAAVDTIVAIMAAGAAHALCVGVMKMSAEDIEKVNKGIGIENIHYLNDGLWHMKTYKAHHHHHH

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	25

Entity 3 Entity 3 non-polymer

Description description	UNKNOWN ATOM OR ION
Source method src_method	syn
Copy count entity_count	174

Entity 4 Entity 4 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 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	1374

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6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id	3r90A00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	400 — Sulfate adenylyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	3r90B00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	400 — Sulfate adenylyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	3r90C00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	400 — Sulfate adenylyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	3r90D00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	400 — Sulfate adenylyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	3r90E00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	400 — Sulfate adenylyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	3r90F00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	400 — Sulfate adenylyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	3r90G00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	400 — Sulfate adenylyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	3r90H00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	400 — Sulfate adenylyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	3r90I00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	400 — Sulfate adenylyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	3r90J00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	400 — Sulfate adenylyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	3r90K00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	400 — Sulfate adenylyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	3r90L00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	400 — Sulfate adenylyltransferase
Homologous superfamily homologous superfamily	20 —

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Unit-cell length a length_a	115.590 Å
Unit-cell length b length_b	115.590 Å
Unit-cell length c length_c	157.790 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	36

Space group space_group	P 31
Space-group number int_tables_number	144
Crystal system crystal_system	—

Resolution resolution	1.700 Å
Low-resolution limit resolution_low	28.420 Å
R factor r_factor	0.2020
R_work r_work	0.2015
R_free r_free	0.2353

Crystal structure of Malignant T cell-amplified sequence 1 protein

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

Malignant T cell-amplified sequence 1

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

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

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) 12 domains

CATH v4.4 (12 domains)

7. Citations (2)

Crystal structure of Malignant T cell-amplified sequence 1 protein

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

Malignant T cell-amplified sequence 1

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

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

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) 12 domains

CATH v4.4 (12 domains)

7. Citations (2)