2ww2

Structure of the Family GH92 Inverting Mannosidase BT2199 from Bacteroides thetaiotaomicron VPI-5482

Method: X-RAY DIFFRACTION

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

ALPHA-1,2-MANNOSIDASE

BACTEROIDES THETAIOTAOMICRON

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 3	(4S)-2-METHYL-2,4-PENTANEDIOL × 1 SODIUM ION × 4 GLYCEROL × 14 1S-8AB-OCTAHYDRO-INDOLIZIDINE-1A,2A,8B-TRIOL × 1 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q8A5N9_BACTN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–737； UniProt 22–758 Author chain B； PDBConstruct 1–737； UniProt 22–758 Author chain C； PDBConstruct 1–737； UniProt 22–758

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	2ww2
Deposition date deposition_date	2009-10-21
Structure title title	Structure of the Family GH92 Inverting Mannosidase BT2199 from Bacteroides thetaiotaomicron VPI-5482
Keywords keywords	HYDROLASE, GLYCOSIDE HYDROLASE FAMILY 92, BT2199; 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.

2ww2__assembly_1__model_1

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

Download this curve (.dat)

2ww2__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2ww2__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	41.62 Å
Rg (electron density)	41.18 Å
Total Rg	41.60 Å
Atom count	17589
Residues	2211
Excluded volume	308430 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2ww2__assembly_1__model_1`	trimeric （3）	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 (6)

Entity 1 Entity 1 polymer

Description description	ALPHA-1,2-MANNOSIDASE
Molecular weight formula_weight	83742.7 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	19766

SKKTVEFVDYVNPLMGTESTFAFSHGNTYPAVAVPWGMNFWSPQTGENGSGWMYTYTDSLMRGFRQTHQPSPWINDYGTFSIMPLAGELKMSHKERLVPFSHQQEKATPYNYSVTFNNGLQTSLSATSRGAVFEVSFPEKEDQYVVVDAYNGGSSITIEPEKRLVKGATRYNNGGVPDNFANYFMMEFSHPVIEYGTYNGDTLLHHQTDVAADYTCAYLKFDVPAGEKLTIRTASSFISPEQAAINFNREVADADVQLISGKAREQWNNYLGRVEAEGGTDEQLRTFYSCLYRTLLFPREFYEFDSQGNPVYYSPYDGNVHDGYMYTDNGFWDTFRAVHPLFTLLYPEVSERVTQSIINAYNESGFMPEWASPGHRGCMIGNNSVSLLVDAWMKGIQTVDAEKALEAMIHQTQARHAEIASVGRDGFEYYDKLGYVPYPEVPEATAKTLEYAYADWCIARFAESLGKQDIADQYYQKAPNYRNLYYPEHGFMWTKDAKGNWRDRFDATEWGGPFTEGSSWHWTWSVFHDPEGLSELMGGHEPMIARLDSMFVAPNTYNYGTYGFVIHEIAEMVALNMGQYAHGNQPVQHAIYLYDYIGQPWKTQYHLRNVMDKLYNSGSKGYCGDEDNGQTSAWYVFSAMGFYPVCPGMPEYAIGSPLFKKVTLHLPEGKNFVVSAADNAADRPYIRKALLNGQEFTRNYLTHDELKQGGELNLSMDSVPNQQRGTQPADFPYSYSK

Source Source

Source organism organism	BACTEROIDES THETAIOTAOMICRON
NCBI taxonomy ID ncbi_taxonomy_id	226186
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	(4S)-2-METHYL-2,4-PENTANEDIOL
Molecular weight formula_weight	118.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	14

Entity 5 Entity 5 non-polymer

Description description	1S-8AB-OCTAHYDRO-INDOLIZIDINE-1A,2A,8B-TRIOL
Molecular weight formula_weight	173.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	2070

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6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id	2ww2A01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2ww2A02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2080 — GH92 mannosidase fold
Homologous superfamily homologous superfamily	10 — GH92 mannosidase domain

Domain ID domain_id	2ww2A03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1050 — Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Homologous superfamily homologous superfamily	60 — alpha-1,2-mannosidase

Domain ID domain_id	2ww2A04
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1610 — Glycosyl hydrolase family fold
Homologous superfamily homologous superfamily	10 — alpha-1,2-mannosidases domains

Domain ID domain_id	2ww2B01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2ww2B02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2080 — GH92 mannosidase fold
Homologous superfamily homologous superfamily	10 — GH92 mannosidase domain

Domain ID domain_id	2ww2B03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1050 — Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Homologous superfamily homologous superfamily	60 — alpha-1,2-mannosidase

Domain ID domain_id	2ww2B04
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1610 — Glycosyl hydrolase family fold
Homologous superfamily homologous superfamily	10 — alpha-1,2-mannosidases domains

Domain ID domain_id	2ww2C01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2ww2C02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2080 — GH92 mannosidase fold
Homologous superfamily homologous superfamily	10 — GH92 mannosidase domain

Domain ID domain_id	2ww2C03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1050 — Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Homologous superfamily homologous superfamily	60 — alpha-1,2-mannosidase

Domain ID domain_id	2ww2C04
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1610 — Glycosyl hydrolase family fold
Homologous superfamily homologous superfamily	10 — alpha-1,2-mannosidases domains

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Unit-cell length a length_a	154.990 Å
Unit-cell length b length_b	162.990 Å
Unit-cell length c length_c	114.860 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	12

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	34.990 Å
R factor r_factor	0.1590
R_work r_work	0.1570
R_free r_free	0.1870

Structure of the Family GH92 Inverting Mannosidase BT2199 from Bacteroides thetaiotaomicron VPI-5482

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

ALPHA-1,2-MANNOSIDASE

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

2ww2__assembly_1__model_1

2ww2__assembly_1__model_1 | I(q)

2ww2__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 (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

7. Citations (1)

Structure of the Family GH92 Inverting Mannosidase BT2199 from Bacteroides thetaiotaomicron VPI-5482

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

ALPHA-1,2-MANNOSIDASE

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

2ww2__assembly_1__model_1

2ww2__assembly_1__model_1 | I(q)

2ww2__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 (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

7. Citations (1)