1k6f

Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3

Method: X-RAY DIFFRACTION

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

No usable UniProt protein identity is available for this entry.

The relationship tables retain this entry's assembly and composition data, but cross-PDB links for the same protein cannot be established reliably without a unified protein identity.

Assembly Composition of the Current Entry

Assembly	Physical composition	Protein state	蛋白 / DNA / RNA / 其他Polymer	Data consistency
1	Protein homooligomer	Homooligomer	3 / 0 / 0 / 0	Consistent with protein count
2	Protein homooligomer	Homooligomer	3 / 0 / 0 / 0	Consistent with protein count
3	Protein homooligomer	Homooligomer	6 / 0 / 0 / 0	Consistent with protein count

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	1k6f
Deposition date deposition_date	2001-10-16
Structure title title	Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3
Keywords keywords	collagen stability, puckering, amino acid preferences, triple helix, STRUCTURAL PROTEIN; STRUCTURAL 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.

1k6f__assembly_1__model_1

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

Download this curve (.dat)

1k6f__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1k6f__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	22.91 Å
Rg (electron density)	24.58 Å
Total Rg	24.48 Å
Atom count	528
Residues	87
Excluded volume	9399 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1k6f__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1k6f__assembly_2__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1k6f__assembly_3__model_1`	hexameric （6）	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 (2)

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6. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (18 domains)

Domain ID domain_id	d1k6fa1
Class class	k — Designed proteins
Fold Fold fold	k.3 — Collagen-like peptides
Superfamily Superfamily superfamily	k.3.1 — Collagen-like peptides
Family Family family	k.3.1.1 — Collagen-like peptides

Domain ID domain_id	d1k6fa2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1k6fa3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1k6fb1
Class class	k — Designed proteins
Fold Fold fold	k.3 — Collagen-like peptides
Superfamily Superfamily superfamily	k.3.1 — Collagen-like peptides
Family Family family	k.3.1.1 — Collagen-like peptides

Domain ID domain_id	d1k6fb2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1k6fb3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1k6fc1
Class class	k — Designed proteins
Fold Fold fold	k.3 — Collagen-like peptides
Superfamily Superfamily superfamily	k.3.1 — Collagen-like peptides
Family Family family	k.3.1.1 — Collagen-like peptides

Domain ID domain_id	d1k6fc2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1k6fc3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1k6fd1
Class class	k — Designed proteins
Fold Fold fold	k.3 — Collagen-like peptides
Superfamily Superfamily superfamily	k.3.1 — Collagen-like peptides
Family Family family	k.3.1.1 — Collagen-like peptides

Domain ID domain_id	d1k6fd2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1k6fd3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1k6fe1
Class class	k — Designed proteins
Fold Fold fold	k.3 — Collagen-like peptides
Superfamily Superfamily superfamily	k.3.1 — Collagen-like peptides
Family Family family	k.3.1.1 — Collagen-like peptides

Domain ID domain_id	d1k6fe2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1k6fe3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1k6ff1
Class class	k — Designed proteins
Fold Fold fold	k.3 — Collagen-like peptides
Superfamily Superfamily superfamily	k.3.1 — Collagen-like peptides
Family Family family	k.3.1.1 — Collagen-like peptides

Domain ID domain_id	d1k6ff2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1k6ff3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

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Unit-cell length a length_a	26.907 Å
Unit-cell length b length_b	26.357 Å
Unit-cell length c length_c	182.498 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	24

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.300 Å
Low-resolution limit resolution_low	15.000 Å
R factor r_factor	0.1850
R_work r_work	0.1810
R_free r_free	0.2970

Description description	collagen triple helix
Molecular weight formula_weight	2530.8 kDa
Source method src_method	syn
Copy count entity_count	6

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	1408

Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3

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

Assembly Composition of the Current Entry

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1k6f__assembly_1__model_1

1k6f__assembly_1__model_1 | I(q)

1k6f__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (18 domains)

7. Citations (4)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	349