SAXSdb — 1w8u

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

NON CATALYTIC PROTEIN 1

PIROMYCES EQUI

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Other combination	Monomer	Protein 1 其他Polymer 1	beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-beta-D-mannopyranose × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9C171
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–145； UniProt 334–478

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	1w8u
Deposition date deposition_date	2004-09-28
Structure title title	CBM29-2 mutant D83A complexed with mannohexaose: Probing the Mechanism of Ligand Recognition by Family 29 Carbohydrate Binding Modules
Keywords keywords	CARBOHYDRATE-BINDING DOMAIN, CARBOHYDRATE BINDING MODULE, GLUCOMANNAN, CELLOHEXAOSE, MANNOHEXAOSE, CELLULOSOME; CARBOHYDRATE-BINDING DOMAIN
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.

1w8u__assembly_1__model_1

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

Download this curve (.dat)

1w8u__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1w8u__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	15.85 Å
Rg (electron density)	14.29 Å
Total Rg	15.54 Å
Atom count	1162
Residues	141
Excluded volume	20483 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1w8u__assembly_1__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 (3)

Entity 1 Entity 1 polymer

Description description	NON CATALYTIC PROTEIN 1
Molecular weight formula_weight	16622.3 kDa
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1350

SNVRATYTVIFKNASGLPNGYDNWGWGCTLSYYGGAMIINPQEGKYGAVSLKRNSGSFRGGSLRFDMKNEGKVKILVENSEAAEKFEVETISPSDEYVTYILDVDFDLPFDRIDFQDAPGNGDRIWIKNLVHSTGSADDFVDPINLEHH

Source Source

Source organism organism	PIROMYCES EQUI
NCBI taxonomy ID ncbi_taxonomy_id	99929
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 branched

Description description	beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-beta-D-mannopyranose
Molecular weight formula_weight	828.7 kDa
Source method src_method	man
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	166

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1w8ua_
Class class	b — All beta proteins
Fold Fold fold	b.18 — Galactose-binding domain-like
Superfamily Superfamily superfamily	b.18.1 — Galactose-binding domain-like
Family Family family	b.18.1.19 — Family 29 carbohydrate binding module, CBM29

CATH v4.4 (1 domains)

Domain ID domain_id	1w8uA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	430 — Galactose-binding lectin

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Unit-cell length a length_a	51.150 Å
Unit-cell length b length_b	42.636 Å
Unit-cell length c length_c	60.182 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	93.71 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	1.300 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.1620
R_work r_work	0.1610
R_free r_free	0.1750

CBM29-2 mutant D83A complexed with mannohexaose: Probing the Mechanism of Ligand Recognition by Family 29 Carbohydrate Binding Modules

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

NON CATALYTIC PROTEIN 1

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

1w8u__assembly_1__model_1

1w8u__assembly_1__model_1 | I(q)

1w8u__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 branched

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)

CBM29-2 mutant D83A complexed with mannohexaose: Probing the Mechanism of Ligand Recognition by Family 29 Carbohydrate Binding Modules

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

NON CATALYTIC PROTEIN 1

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

1w8u__assembly_1__model_1

1w8u__assembly_1__model_1 | I(q)

1w8u__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 branched

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)