SAXSdb — 3av7

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

Putative uncharacterized protein PH0207

Pyrococcus horikoshii

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE × 2 (2S)-2-amino-4-(2-aminophenyl)-4-oxobutanoic acid × 2 4-hydroxyquinoline-2-carboxylic acid × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O57946_PYRHO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 21–448； UniProt 1–428 Author chain C； PDBConstruct 21–448； UniProt 1–428

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	3av7
Deposition date deposition_date	2011-02-23
Structure title title	Crystal structure of Pyrococcus horikoshii kynurenine aminotransferase in complex with PMP, KYN as substrates and KYA as products
Keywords keywords	aminotransferase, PLP binding, transamination, 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.

3av7__assembly_1__model_1

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

Download this curve (.dat)

3av7__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3av7__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	28.57 Å
Rg (electron density)	27.63 Å
Total Rg	28.49 Å
Atom count	6584
Residues	808
Excluded volume	118770 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3av7__assembly_1__model_1`	dimeric （2）	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 (5)

Entity 1 Entity 1 polymer

Description description	Putative uncharacterized protein PH0207
Molecular weight formula_weight	51162.9 kDa
EC 编号 ec_number	2.6.1.7
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	7139

MGSSHHHHHHSSGLVPRGSHMHEDVQLNIYVHSQEGIGMEENIKSMLGDVERFFSKKALEMRASEVRELLKLVETSDIISLAGGLPNPKTFPKEIIRDILVEIMEKYADKALQYGTTKGFTPLRETLMKWLGKRYGISQDNDIMITSGSQQALDLIGRVFLNPGDIVVVEAPTYLAALQAFNFYEPQYIQIPLDDEGMKVEILEEKLKELKSQGKKVKVVYTVPTFQNPAGVTMNEDRRKYLLELASEYDFIVVEDDPYGELRYSGNPEKKIKALDNEGRVIYLGTFSKILAPGFRIGWMVGDPGIIRKMEIAKQSTDLCTNVFGQVVAWRYVDGGYLEKHIPEIRKFYKPRRDAMLEALEEFMPEGVKWTKPEGGMFIWVTLPDGIDSKKMLERAIKKGVAYVPGEAFYAHRDVKNTMRLNFTYVDEDKIMEGIKRLAETIKEELKA

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	4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE
Molecular weight formula_weight	248.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	(2S)-2-amino-4-(2-aminophenyl)-4-oxobutanoic acid
Molecular weight formula_weight	208.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	4-hydroxyquinoline-2-carboxylic acid
Molecular weight formula_weight	189.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	555

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d3av7a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.67 — PLP-dependent transferase-like
Superfamily Superfamily superfamily	c.67.1 — PLP-dependent transferases
Family Family family	c.67.1.0 — automated matches

Domain ID domain_id	d3av7c_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.67 — PLP-dependent transferase-like
Superfamily Superfamily superfamily	c.67.1 — PLP-dependent transferases
Family Family family	c.67.1.0 — automated matches

CATH v4.4 (4 domains)

Domain ID domain_id	3av7A01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily	10 — Aspartate Aminotransferase, domain 1

Domain ID domain_id	3av7A02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	640 — Aspartate Aminotransferase; domain 2
Homologous superfamily homologous superfamily	10 — Type I PLP-dependent aspartate aminotransferase-like (Major domain)

Domain ID domain_id	3av7C01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily	10 — Aspartate Aminotransferase, domain 1

Domain ID domain_id	3av7C02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	640 — Aspartate Aminotransferase; domain 2
Homologous superfamily homologous superfamily	10 — Type I PLP-dependent aspartate aminotransferase-like (Major domain)

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Unit-cell length a length_a	55.619 Å
Unit-cell length b length_b	136.529 Å
Unit-cell length c length_c	55.612 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	100.71 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	1.840 Å
Low-resolution limit resolution_low	26.690 Å
R factor r_factor	0.1793
R_work r_work	0.1762
R_free r_free	0.2379

Crystal structure of Pyrococcus horikoshii kynurenine aminotransferase in complex with PMP, KYN as substrates and KYA as products

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

Putative uncharacterized protein PH0207

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

3av7__assembly_1__model_1

3av7__assembly_1__model_1 | I(q)

3av7__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 (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) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Crystal structure of Pyrococcus horikoshii kynurenine aminotransferase in complex with PMP, KYN as substrates and KYA as products

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

Putative uncharacterized protein PH0207

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

3av7__assembly_1__model_1

3av7__assembly_1__model_1 | I(q)

3av7__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 (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) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (1)