SAXSdb — 1jg1

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

protein-L-isoaspartate O-methyltransferase

Pyrococcus furiosus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	S-ADENOSYL-L-HOMOCYSTEINE × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PIMT_PYRFU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 11–229； UniProt 1–219

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	1jg1
Deposition date deposition_date	2001-06-22
Structure title title	Crystal Structure of L-isoaspartyl (D-aspartyl) O-methyltransferase with S-ADENOSYL-L-HOMOCYSTEINE
Keywords keywords	Rossmann methyltransferase, PROTEIN REPAIR ISOMERIZATION, 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.

1jg1__assembly_1__model_1

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

Download this curve (.dat)

1jg1__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1jg1__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	17.32 Å
Rg (electron density)	16.24 Å
Total Rg	17.35 Å
Atom count	1701
Residues	215
Excluded volume	30926 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1jg1__assembly_1__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 (3)

Entity 1 Entity 1 polymer

Description description	protein-L-isoaspartate O-methyltransferase
Molecular weight formula_weight	26613.1 kDa
EC 编号 ec_number	2.1.1.77
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1957

MHLYSSDFPLMMDEKELYEKWMRTVEMLKAEGIIRSKEVERAFLKYPRYLSVEDKYKKYAHIDEPLPIPAGQTVSAPHMVAIMLEIANLKPGMNILEVGTGSGWNAALISEIVKTDVYTIERIPELVEFAKRNLERAGVKNVHVILGDGSKGFPPKAPYDVIIVTAGAPKIPEPLIEQLKIGGKLIIPVGSYHLWQELLEVRKTKDGIKIKNHGGVAFVPLIGEYGWKEHHHHHH

Source Source

Source organism organism	Pyrococcus furiosus
NCBI taxonomy ID ncbi_taxonomy_id	2261
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	S-ADENOSYL-L-HOMOCYSTEINE
Molecular weight formula_weight	384.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	256

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1jg1a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.66 — S-adenosyl-L-methionine-dependent methyltransferases
Superfamily Superfamily superfamily	c.66.1 — S-adenosyl-L-methionine-dependent methyltransferases
Family Family family	c.66.1.7 — Protein-L-isoaspartyl O-methyltransferase

CATH v4.4 (1 domains)

Domain ID domain_id	1jg1A00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	150 — Vaccinia Virus protein VP39

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Unit-cell length a length_a	39.160 Å
Unit-cell length b length_b	52.522 Å
Unit-cell length c length_c	96.636 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	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.200 Å
Low-resolution limit resolution_low	500.000 Å
R factor r_factor	0.1470
R_work r_work	0.1420
R_free r_free	0.2000

Crystal Structure of L-isoaspartyl (D-aspartyl) O-methyltransferase with S-ADENOSYL-L-HOMOCYSTEINE

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

protein-L-isoaspartate O-methyltransferase

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

1jg1__assembly_1__model_1

1jg1__assembly_1__model_1 | I(q)

1jg1__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)

Crystal Structure of L-isoaspartyl (D-aspartyl) O-methyltransferase with S-ADENOSYL-L-HOMOCYSTEINE

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

protein-L-isoaspartate O-methyltransferase

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

1jg1__assembly_1__model_1

1jg1__assembly_1__model_1 | I(q)

1jg1__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)