SAXSdb — 6fhp

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

Dispase autolysis-inducing protein

Streptomyces mobaraensis

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Thermolysin × 1 （P43133） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Thermolysin × 1 （P43133） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	DAIP_STRMB
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–342； UniProt 31–372 Author chain B； PDBConstruct 1–342； UniProt 31–372

Thermolysin

OrganismNot specified

UniProt P43133

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Dispase autolysis-inducing protein × 1 （P84908） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Dispase autolysis-inducing protein × 1 （P84908） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	THER_GEOSE
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–62； UniProt 490–551 Author chain D； PDBConstruct 1–62； UniProt 490–551

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	6fhp
Deposition date deposition_date	2018-01-15
Structure title title	DAIP in complex with a C-terminal fragment of thermolysin
Keywords keywords	Dispase autolysis-inducing protein; neutral metalloproteases; protease twisting; conformation analysis, ANTIMICROBIAL PROTEIN; ANTIMICROBIAL PROTEIN
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.

6fhp__assembly_1__model_1

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

Download this curve (.dat)

6fhp__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6fhp__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	21.86 Å
Rg (electron density)	20.78 Å
Total Rg	21.76 Å
Atom count	2948
Residues	401
Excluded volume	51693 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6fhp__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`6fhp__assembly_2__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 (3)

Entity 1 Entity 1 polymer

Description description	Dispase autolysis-inducing protein
Molecular weight formula_weight	35536.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	6943

SGWRAPSCTKVTGDGAVTFTTDDGATLAPTTGTLQSVSYTHGLVALDTPNTLLATHNDELQRSTDAGCTWTKVATLGSGSTWLTAATGGRAFAWEKNGGYLARVDGRTVTKLSSPSADIVGVGTDKARRDHVRLAGSDGQLYDSTDAGATWKPLGKLAFGPGASVYTVSFDPADLDHAVAGGMTTGGAVTTDGGATWTAATGLSATAGGKSNLFAASVSPADRNVVYALGIDLVEAAPNSGAEGRHLYRSTDGGRTYTRIVDDTPDTELTNSTLLAPSPVDPNVLYFEYGTYFQAYGTDLYRYDARTGKVGKTHNAHDGISAIAFNPARPSVMYLGLEEVQI

Source Source

Source organism organism	Streptomyces mobaraensis
Common name common_name	Streptoverticillium mobaraense
NCBI taxonomy ID ncbi_taxonomy_id	35621
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Thermolysin
Molecular weight formula_weight	6631.5 kDa
EC 编号 ec_number	3.4.24.27
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

VVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	928

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d6fhpc_
Class class	j — Peptides
Fold Fold fold	j.78 — C-terminal fragment of thermolysin
Superfamily Superfamily superfamily	j.78.1 — C-terminal fragment of thermolysin
Family Family family	j.78.1.1 — C-terminal fragment of thermolysin

Domain ID domain_id	d6fhpd_
Class class	j — Peptides
Fold Fold fold	j.78 — C-terminal fragment of thermolysin
Superfamily Superfamily superfamily	j.78.1 — C-terminal fragment of thermolysin
Family Family family	j.78.1.1 — C-terminal fragment of thermolysin

CATH v4.4 (2 domains)

Domain ID domain_id	6fhpC00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	390 — Neutral Protease; domain 2
Homologous superfamily homologous superfamily	10 — Neutral Protease Domain 2

Domain ID domain_id	6fhpD00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	390 — Neutral Protease; domain 2
Homologous superfamily homologous superfamily	10 — Neutral Protease Domain 2

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Unit-cell length a length_a	64.070 Å
Unit-cell length b length_b	90.050 Å
Unit-cell length c length_c	69.070 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	99.04 °
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	1.703 Å
Low-resolution limit resolution_low	31.148 Å
R factor r_factor	0.1877
R_work r_work	0.1857
R_free r_free	0.2263

DAIP in complex with a C-terminal fragment of thermolysin

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

Dispase autolysis-inducing protein

State in the Current Structure

Other States of the Same Protein in the Database

Thermolysin

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

6fhp__assembly_1__model_1

6fhp__assembly_1__model_1 | I(q)

6fhp__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 polymer

Polymer Polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

DAIP in complex with a C-terminal fragment of thermolysin

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

Dispase autolysis-inducing protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Thermolysin

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

6fhp__assembly_1__model_1

6fhp__assembly_1__model_1 | I(q)

6fhp__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 polymer

Polymer Polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)