SAXSdb — 1iu4

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

microbial transglutaminase

Streptomyces mobaraensis

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
4	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	TGAS_STRMB
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–331； UniProt 46–376 Author chain B； PDBConstruct 1–331； UniProt 46–376 Author chain C； PDBConstruct 1–331； UniProt 46–376 Author chain D； PDBConstruct 1–331； UniProt 46–376

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	1iu4
Deposition date deposition_date	2002-02-27
Structure title title	Crystal Structure Analysis of the Microbial Transglutaminase
Keywords keywords	ALPHA-BETA, TRANSFERASE; TRANSFERASE
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.

1iu4__assembly_3__model_1

Assembly 3 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1iu4__assembly_3__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1iu4__assembly_3__model_1 | P(r) · Pending

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

Rg（Guinier）	21.86 Å
Rg (electron density)	20.67 Å
Total Rg	21.59 Å
Atom count	2678
Residues	331
Excluded volume	46188 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1iu4__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1iu4__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1iu4__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`1iu4__assembly_4__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) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1iu4a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.3 — Cysteine proteinases
Superfamily Superfamily superfamily	d.3.1 — Cysteine proteinases
Family Family family	d.3.1.8 — Microbial transglutaminase

Domain ID domain_id	d1iu4b_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.3 — Cysteine proteinases
Superfamily Superfamily superfamily	d.3.1 — Cysteine proteinases
Family Family family	d.3.1.8 — Microbial transglutaminase

Domain ID domain_id	d1iu4c_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.3 — Cysteine proteinases
Superfamily Superfamily superfamily	d.3.1 — Cysteine proteinases
Family Family family	d.3.1.8 — Microbial transglutaminase

Domain ID domain_id	d1iu4d_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.3 — Cysteine proteinases
Superfamily Superfamily superfamily	d.3.1 — Cysteine proteinases
Family Family family	d.3.1.8 — Microbial transglutaminase

CATH v4.4 (4 domains)

Domain ID domain_id	1iu4A00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1360 — Microbial transglutaminase. Chain: a
Homologous superfamily homologous superfamily	10 — Protein-glutamine gamma-glutamyltransferase

Domain ID domain_id	1iu4B00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1360 — Microbial transglutaminase. Chain: a
Homologous superfamily homologous superfamily	10 — Protein-glutamine gamma-glutamyltransferase

Domain ID domain_id	1iu4C00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1360 — Microbial transglutaminase. Chain: a
Homologous superfamily homologous superfamily	10 — Protein-glutamine gamma-glutamyltransferase

Domain ID domain_id	1iu4D00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1360 — Microbial transglutaminase. Chain: a
Homologous superfamily homologous superfamily	10 — Protein-glutamine gamma-glutamyltransferase

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Unit-cell length a length_a	78.410 Å
Unit-cell length b length_b	117.120 Å
Unit-cell length c length_c	85.740 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	112.80 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

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

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	40.000 Å
R factor r_factor	0.2026
R_work r_work	0.1991
R_free r_free	0.2662

Description description	microbial transglutaminase
Molecular weight formula_weight	37918.4 kDa
EC 编号 ec_number	2.3.2.13
Source method src_method	man
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	11262

Crystal Structure Analysis of the Microbial Transglutaminase

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

microbial transglutaminase

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

1iu4__assembly_3__model_1

1iu4__assembly_3__model_1 | I(q)

1iu4__assembly_3__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) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Source organism organism	Streptomyces mobaraensis
NCBI taxonomy ID ncbi_taxonomy_id	35621
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	550

Crystal Structure Analysis of the Microbial Transglutaminase

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

microbial transglutaminase

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

1iu4__assembly_3__model_1

1iu4__assembly_3__model_1 | I(q)

1iu4__assembly_3__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) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)