SAXSdb — 2rfw

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

Cellulose 1,4-beta-cellobiosidase

Melanocarpus albomyces

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
4	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q8J0K6_MELAO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–430； UniProt 23–452 Author chain B； PDBConstruct 1–430； UniProt 23–452 Author chain C； PDBConstruct 1–430； UniProt 23–452 Author chain D； PDBConstruct 1–430； UniProt 23–452

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	2rfw
Deposition date deposition_date	2007-10-02
Structure title title	Crystal Structure of Cellobiohydrolase from Melanocarpus albomyces
Keywords keywords	hydrolase, Glycosidase; 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.

2rfw__assembly_4__model_1

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

Download this curve (.dat)

2rfw__assembly_4__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2rfw__assembly_4__model_1 | P(r) · Pending

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

Rg（Guinier）	21.74 Å
Rg (electron density)	20.53 Å
Total Rg	21.42 Å
Atom count	3333
Residues	429
Excluded volume	57964 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2rfw__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2rfw__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2rfw__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`2rfw__assembly_4__model_1`	monomeric （1）	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)

Entity 1 Entity 1 polymer

Description description	Cellulose 1,4-beta-cellobiosidase
Molecular weight formula_weight	47572.2 kDa
EC 编号 ec_number	3.2.1.91
Mutation mutation	Q1(PCA)
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	14021

QRAGNETPENHPPLTWQRCTAPGNCQTVNAEVVIDANWRWLHDDNMQNCYDGNQWTNACSTATDCAEKCMIEGAGDYLGTYGASTSGDALTLKFVTKHEYGTNVGSRFYLMNGPDKYQMFNLMGNELAFDVDLSTVECGINSALYFVAMEEDGGMASYPSNQAGARYGTGYCDAQCARDLKFVGGKANIEGWKSSTSDPNAGVGPYGSCCAEIDVWESNAYAFAFTPHACTTNEYHVCETTNCGGTYSEDRFAGKCDANGCDYNPYRMGNPDFYGKGKTLDTSRKFTVVSRFEENKLSQYFIQDGRKIEIPPPTWEGMPNSSEITPELCSTMFDVFNDRNRFEEVGGFEQLNNALRVPMVLVMSIWDDHYANMLWLDSIYPPEKEGQPGAARGDCPTDSGVPAEVEAQFPDAQVVWSNIRFGPIGSTYDF

Source Source

Source organism organism	Melanocarpus albomyces
NCBI taxonomy ID ncbi_taxonomy_id	204285
Host organism host_organism	Trichoderma reesei

Entity 2 Entity 2 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	689

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2rfwa_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.0 — automated matches

Domain ID domain_id	d2rfwb_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.0 — automated matches

Domain ID domain_id	d2rfwc_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.0 — automated matches

Domain ID domain_id	d2rfwd_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.0 — automated matches

CATH v4.4 (4 domains)

Domain ID domain_id	2rfwA00
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	100 — 1,4-Beta-D-Glucan Cellobiohydrolase I; Chain A
Homologous superfamily homologous superfamily	10 — Glycoside hydrolase, family 7, domain

Domain ID domain_id	2rfwB00
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	100 — 1,4-Beta-D-Glucan Cellobiohydrolase I; Chain A
Homologous superfamily homologous superfamily	10 — Glycoside hydrolase, family 7, domain

Domain ID domain_id	2rfwC00
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	100 — 1,4-Beta-D-Glucan Cellobiohydrolase I; Chain A
Homologous superfamily homologous superfamily	10 — Glycoside hydrolase, family 7, domain

Domain ID domain_id	2rfwD00
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	100 — 1,4-Beta-D-Glucan Cellobiohydrolase I; Chain A
Homologous superfamily homologous superfamily	10 — Glycoside hydrolase, family 7, domain

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Unit-cell length a length_a	50.940 Å
Unit-cell length b length_b	94.520 Å
Unit-cell length c length_c	189.850 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	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.600 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1990
R_work r_work	—
R_free r_free	0.2430

Crystal Structure of Cellobiohydrolase from Melanocarpus albomyces

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

Cellulose 1,4-beta-cellobiosidase

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

2rfw__assembly_4__model_1

2rfw__assembly_4__model_1 | I(q)

2rfw__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Crystal Structure of Cellobiohydrolase from Melanocarpus albomyces

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

Cellulose 1,4-beta-cellobiosidase

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

2rfw__assembly_4__model_1

2rfw__assembly_4__model_1 | I(q)

2rfw__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)