SAXSdb — 1e5s

▼

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

PROLINE OXIDASE

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	SULFATE ION × 1 FE (II) ION × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O09345
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–290； UniProt 1–290 Author chain B； PDBConstruct 1–290； UniProt 1–290

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1e5s
Deposition date deposition_date	2000-07-28
Structure title title	Proline 3-hydroxylase (type II) - Iron form
Keywords keywords	OXYGENASE, 2-OXOGLUTARATE DEPENDENT OXYGENASE; OXYGENASE
Experimental Method method	X-RAY DIFFRACTION

▼

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.

1e5s__assembly_1__model_1

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

Download this curve (.dat)

1e5s__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1e5s__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	31.68 Å
Rg (electron density)	31.22 Å
Total Rg	31.70 Å
Atom count	4082
Residues	503
Excluded volume	72496 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1e5s__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	PROLINE OXIDASE
Molecular weight formula_weight	33618.8 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	4298

MRSHILGKIELDQTRLAPDLAYLAAVPTVEEEYDEFSNGFWKHVPLWNASGDSEDRLYRDLKDAAAQPTAHVEHVPYLKEIVTTVFDGTHLQMARSRNLKNAIVIPHRDFVELDREVDRYFRTFMVLEDSPLAFHSNEDTVIHMRPGEIWFLDAATVHSAVNFSEISRQSLCVDFAFDGPFDEKEIFADATLYAPGSTPDLPERRPFTAEHRRRILSLGQVIERENFRDILFLLSKVHYKYDVHPSETYDWLIEISKQAGDEKMVVKAEQIRDFAVEARALSERFSLTSW

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	1

Entity 3 Entity 3 non-polymer

Description description	FE (II) ION
Molecular weight formula_weight	55.8 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	216

▼

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1e5sa_
Class class	b — All beta proteins
Fold Fold fold	b.82 — Double-stranded beta-helix
Superfamily Superfamily superfamily	b.82.2 — Clavaminate synthase-like
Family Family family	b.82.2.4 — Type II Proline 3-hydroxylase (proline oxidase)

Domain ID domain_id	d1e5sb_
Class class	b — All beta proteins
Fold Fold fold	b.82 — Double-stranded beta-helix
Superfamily Superfamily superfamily	b.82.2 — Clavaminate synthase-like
Family Family family	b.82.2.4 — Type II Proline 3-hydroxylase (proline oxidase)

CATH v4.4 (4 domains)

Domain ID domain_id	1e5sA01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	330 — B-lactam Antibiotic, Isopenicillin N Synthase; Chain

Domain ID domain_id	1e5sA02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1720 — Proline Oxidase; Chain: A, Domain 2
Homologous superfamily homologous superfamily	10 — L-proline 3-hydroxylase, C-terminal domain

Domain ID domain_id	1e5sB01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	330 — B-lactam Antibiotic, Isopenicillin N Synthase; Chain

Domain ID domain_id	1e5sB02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1720 — Proline Oxidase; Chain: A, Domain 2
Homologous superfamily homologous superfamily	10 — L-proline 3-hydroxylase, C-terminal domain

▶

Unit-cell length a length_a	72.780 Å
Unit-cell length b length_b	72.780 Å
Unit-cell length c length_c	224.900 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	12

Space group space_group	P 31 2 1
Space-group number int_tables_number	152
Crystal system crystal_system	—

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	23.820 Å
R factor r_factor	0.2160
R_work r_work	0.2160
R_free r_free	0.2710

Proline 3-hydroxylase (type II) - Iron form

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

PROLINE OXIDASE

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

1e5s__assembly_1__model_1

1e5s__assembly_1__model_1 | I(q)

1e5s__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Proline 3-hydroxylase (type II) - Iron form

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

PROLINE OXIDASE

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

1e5s__assembly_1__model_1

1e5s__assembly_1__model_1 | I(q)

1e5s__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (1)