SAXSdb — 4cd7

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

ENDO-BETA-1,4-MANNANASE

ALICYCLOBACILLUS ACIDOCALDARIUS

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)-alpha-D-mannopyranose × 1 5-HYDROXYMETHYL-3,4-DIHYDROXYPIPERIDINE × 1 beta-D-mannopyranose × 1 water × 1	Consistent with protein count
2	Other combination	Monomer	Protein 1 其他Polymer 1	beta-D-mannopyranose-(1-4)-alpha-D-mannopyranose × 1 5-HYDROXYMETHYL-3,4-DIHYDROXYPIPERIDINE × 1 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	A5H1I6_9BACL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–320； UniProt 1–320 Author chain B； PDBConstruct 1–320； UniProt 1–320

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	4cd7
Deposition date deposition_date	2013-10-30
Structure title title	The structure of GH113 beta-mannanase AaManA from Alicyclobacillus acidocaldarius in complex with ManIFG and beta-1,4-mannobiose
Keywords keywords	;HYDROLASE, BETA-MANNOSIDASE, MANNOSIDASE, GLYCOSIDE HYDROLASE, GH26, GH113, CAZY, ENZYME-CARBOHYDRATE INTERACTION, GLYCOSIDASE INHIBITION, QUANTUM MECHANICS, BIOCATALYSIS, CONFORMATION ;; 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.

4cd7__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

4cd7__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4cd7__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	19.58 Å
Rg (electron density)	18.32 Å
Total Rg	19.17 Å
Atom count	2527
Residues	314
Excluded volume	44355 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4cd7__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`4cd7__assembly_2__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 (5)

Entity 1 Entity 1 polymer

Description description	ENDO-BETA-1,4-MANNANASE
Molecular weight formula_weight	36343.0 kDa
EC 编号 ec_number	3.2.1.78
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	5595

MGRIESAFDLGFIRGMTFGFVGQHGTWGTDEARASMRALAEQPFNWVTLAFAGLMEHPGDPAIAYGPPVTVSDDEIASMAELAHALGLKVCLKPTVNCRDGTWRGEIRFEKEHGPDLESWEAWFGSYSDMMAHYAHVAKRTGCEMFCVGCEMTTAEPHEAMWRETIARVRTEYDGLVTYNCNHGREEHVRFWDAVDLISSSAYYPIDRWRDRVPVLREVAEAHEKPLFFMEVGCPSRSGSGACPWDYRHPGAVCLDEQARFYEAMFAAMPDEPWFKGYMLWEWPWKLYPREAASEDGSYCIYGKPAEDVVARAFSAIANR

Source Source

Source organism organism	ALICYCLOBACILLUS ACIDOCALDARIUS
NCBI taxonomy ID ncbi_taxonomy_id	405212
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 branched

Description description	beta-D-mannopyranose-(1-4)-alpha-D-mannopyranose
Molecular weight formula_weight	342.3 kDa
Source method src_method	man
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	5-HYDROXYMETHYL-3,4-DIHYDROXYPIPERIDINE
Molecular weight formula_weight	147.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	beta-D-mannopyranose
Molecular weight formula_weight	180.2 kDa
Source method src_method	man
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	470

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6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id	4cd7A00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	80 — Glycosidases

Domain ID domain_id	4cd7B00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	80 — Glycosidases

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Unit-cell length a length_a	69.472 Å
Unit-cell length b length_b	76.586 Å
Unit-cell length c length_c	140.212 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 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.650 Å
Low-resolution limit resolution_low	70.110 Å
R factor r_factor	0.1531
R_work r_work	0.1508
R_free r_free	0.1962

The structure of GH113 beta-mannanase AaManA from Alicyclobacillus acidocaldarius in complex with ManIFG and beta-1,4-mannobiose

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

ENDO-BETA-1,4-MANNANASE

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

4cd7__assembly_2__model_1

4cd7__assembly_2__model_1 | I(q)

4cd7__assembly_2__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 branched

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

7. Citations (1)

The structure of GH113 beta-mannanase AaManA from Alicyclobacillus acidocaldarius in complex with ManIFG and beta-1,4-mannobiose

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

ENDO-BETA-1,4-MANNANASE

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

4cd7__assembly_2__model_1

4cd7__assembly_2__model_1 | I(q)

4cd7__assembly_2__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 branched

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

7. Citations (1)