SAXSdb — 4gxp

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

Beta-glucosidase Chimeric protein

Trichoderma reesei

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Monomer	Protein 1	water × 1	Consistent with protein count
2	Insufficient information	Monomer	Protein 1	water × 1	Consistent with protein count
3	Insufficient information	Monomer	Protein 1	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	O93785_HYPJE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 168–210； UniProt 160–202 Author chain A； PDBConstruct 225–371； UniProt 221–367 Author chain A； PDBConstruct 401–415； UniProt 399–413 Author chain B； PDBConstruct 168–210； UniProt 160–202 Author chain B； PDBConstruct 225–371； UniProt 221–367 Author chain B； PDBConstruct 401–415； UniProt 399–413 Author chain C； PDBConstruct 168–210； UniProt 160–202 Author chain C； PDBConstruct 225–371； UniProt 221–367 Author chain C； PDBConstruct 401–415； UniProt 399–413

Beta-glucosidase Chimeric protein

Trichoderma reesei

UniProt Q08638

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Monomer	Protein 1	water × 1	Consistent with protein count
2	Insufficient information	Monomer	Protein 1	water × 1	Consistent with protein count
3	Insufficient information	Monomer	Protein 1	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	BGLA_THEMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 8–167； UniProt 1–160 Author chain A； PDBConstruct 211–224； UniProt 204–217 Author chain A； PDBConstruct 372–400； UniProt 352–380 Author chain A； PDBConstruct 416–467； UniProt 395–446 Author chain B； PDBConstruct 8–167； UniProt 1–160 Author chain B； PDBConstruct 211–224； UniProt 204–217 Author chain B； PDBConstruct 372–400； UniProt 352–380 Author chain B； PDBConstruct 416–467； UniProt 395–446 Author chain C； PDBConstruct 8–167； UniProt 1–160 Author chain C； PDBConstruct 211–224； UniProt 204–217 Author chain C； PDBConstruct 372–400； UniProt 352–380 Author chain C； PDBConstruct 416–467； UniProt 395–446

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	4gxp
Deposition date deposition_date	2012-09-04
Structure title title	Chimeric Family 1 beta-glucosidase made with non-contiguous SCHEMA
Keywords keywords	chimeragenesis, protein recombination, eukaryotic-prokaryotic chimera, GH1, beta-glucosidase, HYDROLASE; 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.

4gxp__assembly_1__model_1

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

Download this curve (.dat)

4gxp__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4gxp__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	22.02 Å
Rg (electron density)	20.64 Å
Total Rg	21.58 Å
Atom count	3451
Residues	456
Excluded volume	59947 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4gxp__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`4gxp__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`4gxp__assembly_3__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	Beta-glucosidase Chimeric protein
Molecular weight formula_weight	53026.3 kDa
EC 编号 ec_number	3.2.1.21
Mutation mutation	Y120F,W134L,A135L,H378Y,Q336A,S337M
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	9869

MHHHHHHMNVKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTGDVACDHYNRWKEDIEIIEKLGVKAYRFSISWPRILPEGTGRVNQKGLDFYNRIIDTLLEKGITPFVTIFHWDLPFALQLKGGLLNREIADWFAEYSRVLFENFGDRVKNWITFNEPLCSAIPGYGSGTFAPGRQSTSEPWTVGHNILVAHGRAVKVFRETVKDGKIGIVLNGDFTYPWDAADPADKEAAERRLEFFTAWFADPIYLGDYPASMRKQLGDRLPTFTPEERALVHGSNDFYGMNHYTSNYIRHRSSPASADDTVGNVDVLFTNKQGNCIGPETAMPWLRPCAAGFRDFLVWISKRYGYPPIYVTENGAAFDDVVSEDGRVHDQNRIDYLKAYIGAMVTAVELDGVNVKGYFVWSLLDNFEWAEGYSKRFGIVYVDYSTQKRIVKDSGYWYSNVVKNNGLED

Source Source

Source organism organism	Trichoderma reesei
NCBI taxonomy ID ncbi_taxonomy_id	51453
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	2

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d4gxpa_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.8 — (Trans)glycosidases
Family Family family	c.1.8.4 — Family 1 of glycosyl hydrolase

Domain ID domain_id	d4gxpb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.8 — (Trans)glycosidases
Family Family family	c.1.8.4 — Family 1 of glycosyl hydrolase

Domain ID domain_id	d4gxpc_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.8 — (Trans)glycosidases
Family Family family	c.1.8.4 — Family 1 of glycosyl hydrolase

CATH v4.4 (3 domains)

Domain ID domain_id	4gxpA00
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	4gxpB00
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	4gxpC00
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	115.377 Å
Unit-cell length b length_b	115.377 Å
Unit-cell length c length_c	282.538 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	18

Space group space_group	P 31 1 2
Space-group number int_tables_number	151
Crystal system crystal_system	—

Resolution resolution	3.000 Å
Low-resolution limit resolution_low	37.430 Å
R factor r_factor	0.2416
R_work r_work	0.2389
R_free r_free	0.2938

Chimeric Family 1 beta-glucosidase made with non-contiguous SCHEMA

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

Beta-glucosidase Chimeric protein

State in the Current Structure

Other States of the Same Protein in the Database

Beta-glucosidase Chimeric protein

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

4gxp__assembly_1__model_1

4gxp__assembly_1__model_1 | I(q)

4gxp__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (1)

Chimeric Family 1 beta-glucosidase made with non-contiguous SCHEMA

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

Beta-glucosidase Chimeric protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Beta-glucosidase Chimeric protein

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

4gxp__assembly_1__model_1

4gxp__assembly_1__model_1 | I(q)

4gxp__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (1)