2y3n

Type II cohesin-dockerin domain from Bacteroides cellolosolvens

Method: X-RAY DIFFRACTION

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

CELLULOSOMAL SCAFFOLDIN

BACTEROIDES CELLULOSOLVENS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	CELLULOSOMAL FAMILY-48 PROCESSIVE GLYCOSIDE HYDROLASE × 1 （Q6UB36） CALCIUM ION × 2 water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	CELLULOSOMAL FAMILY-48 PROCESSIVE GLYCOSIDE HYDROLASE × 1 （Q6UB36） CALCIUM ION × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9FDJ9_9FIRM
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–173； UniProt 2073–2242 Author chain C； PDBConstruct 4–173； UniProt 2073–2242

CELLULOSOMAL FAMILY-48 PROCESSIVE GLYCOSIDE HYDROLASE

BACTEROIDES CELLULOSOLVENS

UniProt Q6UB36

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	CELLULOSOMAL SCAFFOLDIN × 1 （Q9FDJ9） CALCIUM ION × 2 water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	CELLULOSOMAL SCAFFOLDIN × 1 （Q9FDJ9） CALCIUM ION × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q6UB36_9FIRM
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 2–71； UniProt 683–752 Author chain D； PDBConstruct 2–71； UniProt 683–752

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	2y3n
Deposition date deposition_date	2010-12-22
Structure title title	Type II cohesin-dockerin domain from Bacteroides cellolosolvens
Keywords keywords	STRUCTRUAL PROTEIN-HYDROLASE COMPLEX, CELLULOSOME; STRUCTRUAL PROTEIN/HYDROLASE
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.

2y3n__assembly_1__model_1

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

Download this curve (.dat)

2y3n__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2y3n__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	18.28 Å
Rg (electron density)	17.51 Å
Total Rg	18.50 Å
Atom count	1687
Residues	220
Excluded volume	30207 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2y3n__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2y3n__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 (4)

Entity 1 Entity 1 polymer

Description description	CELLULOSOMAL SCAFFOLDIN
Molecular weight formula_weight	20030.5 kDa
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	3765

MASGSVLTAIDNDKVAVGDKVTLTINVDKITNFSGYQFNIKYNTTYLQPWDTIADEAYTDSTMPDYGTLLQGRFNATDMSKHNLSQGVLNFGRLYMNLSAYRASGKPESTGAVAKVTFKVIKEIPAEGIKLATFENGSSMNNAVDGTMLFDWDGNMYSSSAYKVVQPGLIYPKLEHHHHHH

Source Source

Source organism organism	BACTEROIDES CELLULOSOLVENS
NCBI taxonomy ID ncbi_taxonomy_id	35825
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	CELLULOSOMAL FAMILY-48 PROCESSIVE GLYCOSIDE HYDROLASE
Molecular weight formula_weight	7540.6 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

MFVKLKGDLNGDGVINMADVMILAQSFGKAIGNPGVNEKADLNNDGVINSDDAIILAQYFGKTKSAEVVMF

Source Source

Source organism organism	BACTEROIDES CELLULOSOLVENS
NCBI taxonomy ID ncbi_taxonomy_id	35825
Host organism host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	299

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6. Fold Classification (SCOP + CATH) 13 domains

SCOP 2.08 (9 domains)

Domain ID domain_id	d2y3na1
Class class	b — All beta proteins
Fold Fold fold	b.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamily	b.2.2 — Carbohydrate-binding domain
Family Family family	b.2.2.2 — Cellulose-binding domain family III

Domain ID domain_id	d2y3na2
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	d2y3na3
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	d2y3nb1
Class class	a — All alpha proteins
Fold Fold fold	a.139 — Type I dockerin domain
Superfamily Superfamily superfamily	a.139.1 — Type I dockerin domain
Family Family family	a.139.1.0 — automated matches

Domain ID domain_id	d2y3nb2
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	d2y3nc1
Class class	b — All beta proteins
Fold Fold fold	b.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamily	b.2.2 — Carbohydrate-binding domain
Family Family family	b.2.2.2 — Cellulose-binding domain family III

Domain ID domain_id	d2y3nc2
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	d2y3nd1
Class class	a — All alpha proteins
Fold Fold fold	a.139 — Type I dockerin domain
Superfamily Superfamily superfamily	a.139.1 — Type I dockerin domain
Family Family family	a.139.1.0 — automated matches

Domain ID domain_id	d2y3nd2
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

CATH v4.4 (4 domains)

Domain ID domain_id	2y3nA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	680 —

Domain ID domain_id	2y3nB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1330 — Type 1 dockerin domain
Homologous superfamily homologous superfamily	10 — Dockerin domain

Domain ID domain_id	2y3nC00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	680 —

Domain ID domain_id	2y3nD00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1330 — Type 1 dockerin domain
Homologous superfamily homologous superfamily	10 — Dockerin domain

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Unit-cell length a length_a	43.410 Å
Unit-cell length b length_b	116.120 Å
Unit-cell length c length_c	45.160 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	112.45 °
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	1.900 Å
Low-resolution limit resolution_low	41.740 Å
R factor r_factor	0.1664
R_work r_work	0.1633
R_free r_free	0.2249

Type II cohesin-dockerin domain from Bacteroides cellolosolvens

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

CELLULOSOMAL SCAFFOLDIN

State in the Current Structure

Other States of the Same Protein in the Database

CELLULOSOMAL FAMILY-48 PROCESSIVE GLYCOSIDE HYDROLASE

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

2y3n__assembly_1__model_1

2y3n__assembly_1__model_1 | I(q)

2y3n__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

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 13 domains

SCOP 2.08 (9 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Type II cohesin-dockerin domain from Bacteroides cellolosolvens

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

CELLULOSOMAL SCAFFOLDIN

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

CELLULOSOMAL FAMILY-48 PROCESSIVE GLYCOSIDE HYDROLASE

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

2y3n__assembly_1__model_1

2y3n__assembly_1__model_1 | I(q)

2y3n__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

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 13 domains

SCOP 2.08 (9 domains)

CATH v4.4 (4 domains)

7. Citations (1)