SAXSdb — 2wr8

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

PUTATIVE UNCHARACTERIZED PROTEIN PH0463

PYROCOCCUS HORIKOSHII

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 3	S-ADENOSYL-L-HOMOCYSTEINE × 3 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O58212_PYRHO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–259； UniProt 1–256

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	2wr8
Deposition date deposition_date	2009-08-31
Structure title title	Structure of Pyrococcus horikoshii SAM hydroxide adenosyltransferase in complex with SAH
Keywords keywords	TRANSFERASE, SAM, SAM HYDROXIDE ADENOSYLTRANSFERASE (DUF-62), SN2, WATER ACTIVATION; 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.

2wr8__assembly_1__model_1

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

Download this curve (.dat)

2wr8__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2wr8__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	27.76 Å
Rg (electron density)	26.63 Å
Total Rg	27.53 Å
Atom count	6171
Residues	774
Excluded volume	111100 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2wr8__assembly_1__model_1`	trimeric （3）	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	PUTATIVE UNCHARACTERIZED PROTEIN PH0463
Molecular weight formula_weight	28934.5 kDa
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	2179

GSHMITLTTDFGLKGPYVGEMKVAMLRINPNAKIVDVTHSVTRHSILEGSFVMEQVVKYSPKGTVHVGVIDPGVGTERRAIVIEGDQYLVVPDNGLATLPLKHIKVKSVYEIIPDKIRKFTGWEISSTFHGRDIFGPAGALIEKGIHPEEFGREIPVDSIVKLNVEPRKEGDVWILKVIYIDDFGNVILNLENYEKPRTVELLDFNLRLPYLETYGLVEKGEMLALPGSHDYLEIAVNMGSAAERLNVKVGDELRVRLL

Source Source

Source organism organism	PYROCOCCUS HORIKOSHII
NCBI taxonomy ID ncbi_taxonomy_id	70601
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	115

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6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id	2wr8A01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10790 — S-adenosyl-l-methionine hydroxide adenosyltransferase, N-terminal

Domain ID domain_id	2wr8A02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	90 — Bacterial fluorinating enzyme like

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Unit-cell length a length_a	65.561 Å
Unit-cell length b length_b	65.561 Å
Unit-cell length c length_c	142.685 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	9

Space group space_group	H 3
Space-group number int_tables_number	146
Crystal system crystal_system	—

Resolution resolution	1.770 Å
Low-resolution limit resolution_low	52.780 Å
R factor r_factor	0.1704
R_work r_work	0.1680
R_free r_free	0.2174

Structure of Pyrococcus horikoshii SAM hydroxide adenosyltransferase in complex with SAH

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

PUTATIVE UNCHARACTERIZED PROTEIN PH0463

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

2wr8__assembly_1__model_1

2wr8__assembly_1__model_1 | I(q)

2wr8__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

CATH v4.4 (2 domains)

7. Citations (1)

Structure of Pyrococcus horikoshii SAM hydroxide adenosyltransferase in complex with SAH

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

PUTATIVE UNCHARACTERIZED PROTEIN PH0463

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

2wr8__assembly_1__model_1

2wr8__assembly_1__model_1 | I(q)

2wr8__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

CATH v4.4 (2 domains)

7. Citations (1)