2pro

PRO REGION OF ALPHA-LYTIC PROTEASE

Method: X-RAY DIFFRACTION

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

ALPHA-LYTIC PROTEASE

Lysobacter enzymogenes

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	No other associated polymer	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	No other associated polymer	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	No other associated polymer	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 3	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PRLA_LYSEN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–166； UniProt 34–199 Author chain B； PDBConstruct 1–166； UniProt 34–199 Author chain C； PDBConstruct 1–166； UniProt 34–199

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	2pro
Deposition date deposition_date	1998-08-20
Structure title title	PRO REGION OF ALPHA-LYTIC PROTEASE
Keywords keywords	PRO REGION, FOLDASE, PROTEIN FOLDING, SERINE PROTEASE; PRO REGION
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.

2pro__assembly_4__model_1

Assembly 4 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2pro__assembly_4__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2pro__assembly_4__model_1 | P(r) · Pending

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

Rg（Guinier）	27.77 Å
Rg (electron density)	26.76 Å
Total Rg	27.42 Å
Atom count	3139
Residues	414
Excluded volume	55209 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2pro__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2pro__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2pro__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`2pro__assembly_4__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 (1)

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d2proa1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.52 — Alpha-lytic protease prodomain-like
Superfamily Superfamily superfamily	d.52.1 — Alpha-lytic protease prodomain
Family Family family	d.52.1.1 — Alpha-lytic protease prodomain

Domain ID domain_id	d2proa2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.52 — Alpha-lytic protease prodomain-like
Superfamily Superfamily superfamily	d.52.1 — Alpha-lytic protease prodomain
Family Family family	d.52.1.1 — Alpha-lytic protease prodomain

Domain ID domain_id	d2prob1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.52 — Alpha-lytic protease prodomain-like
Superfamily Superfamily superfamily	d.52.1 — Alpha-lytic protease prodomain
Family Family family	d.52.1.1 — Alpha-lytic protease prodomain

Domain ID domain_id	d2prob2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.52 — Alpha-lytic protease prodomain-like
Superfamily Superfamily superfamily	d.52.1 — Alpha-lytic protease prodomain
Family Family family	d.52.1.1 — Alpha-lytic protease prodomain

Domain ID domain_id	d2proc1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.52 — Alpha-lytic protease prodomain-like
Superfamily Superfamily superfamily	d.52.1 — Alpha-lytic protease prodomain
Family Family family	d.52.1.1 — Alpha-lytic protease prodomain

Domain ID domain_id	d2proc2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.52 — Alpha-lytic protease prodomain-like
Superfamily Superfamily superfamily	d.52.1 — Alpha-lytic protease prodomain
Family Family family	d.52.1.1 — Alpha-lytic protease prodomain

CATH v4.4 (6 domains)

Domain ID domain_id	2proA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily	50 —

Domain ID domain_id	2proA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily	50 —

Domain ID domain_id	2proB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily	50 —

Domain ID domain_id	2proB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily	50 —

Domain ID domain_id	2proC01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily	50 —

Domain ID domain_id	2proC02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily	50 —

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Unit-cell length a length_a	47.600 Å
Unit-cell length b length_b	54.700 Å
Unit-cell length c length_c	64.000 Å
Unit-cell angle α angle_alpha	104.00 °
Unit-cell angle β angle_beta	102.50 °
Unit-cell angle γ angle_gamma	91.90 °
Molecules per unit cell Z z_pdb	3

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

Resolution resolution	3.000 Å
Low-resolution limit resolution_low	6.000 Å
R factor r_factor	0.2020
R_work r_work	0.2020
R_free r_free	0.3420

Description description	ALPHA-LYTIC PROTEASE
Molecular weight formula_weight	17835.9 kDa
Source method src_method	man
Copy count entity_count	3

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	3139

PRO REGION OF ALPHA-LYTIC PROTEASE

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

ALPHA-LYTIC PROTEASE

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

2pro__assembly_4__model_1

2pro__assembly_4__model_1 | I(q)

2pro__assembly_4__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (1)

Source organism organism	Lysobacter enzymogenes
NCBI taxonomy ID ncbi_taxonomy_id	69
Host organism host_organism	Escherichia coli

PRO REGION OF ALPHA-LYTIC PROTEASE

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

ALPHA-LYTIC PROTEASE

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

2pro__assembly_4__model_1

2pro__assembly_4__model_1 | I(q)

2pro__assembly_4__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (1)