SAXSdb — 4xtc

▼

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

AlgM1

Sphingomonas sp. A1

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Other combination	Heteromer	Protein 5 其他Polymer 1	AlgM2 × 1 （Q9KWT7） AlgS × 2 （Q9KWT9） AlgQ2 × 1 （Q9KWT5） ;beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid ; × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9KWT8_SPHSX
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain M； PDBConstruct 1–301； UniProt 1–324

AlgM2

Sphingomonas sp. A1

UniProt Q9KWT7

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Other combination	Heteromer	Protein 5 其他Polymer 1	AlgM1 × 1 （Q9KWT8） AlgS × 2 （Q9KWT9） AlgQ2 × 1 （Q9KWT5） ;beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid ; × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9KWT7_SPHSX
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain N； PDBConstruct 1–293； UniProt 1–293

AlgS

Sphingomonas sp. A1

UniProt Q9KWT9

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Other combination	Heteromer	Protein 5 其他Polymer 1	AlgM1 × 1 （Q9KWT8） AlgM2 × 1 （Q9KWT7） AlgQ2 × 1 （Q9KWT5） ;beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid ; × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9KWT9_SPHSX
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain S； PDBConstruct 1–363； UniProt 1–363 Author chain T； PDBConstruct 1–363； UniProt 1–363

AlgQ2

Sphingomonas sp. A1

UniProt Q9KWT5

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Other combination	Heteromer	Protein 5 其他Polymer 1	AlgM1 × 1 （Q9KWT8） AlgM2 × 1 （Q9KWT7） AlgS × 2 （Q9KWT9） ;beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid ; × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9KWT5_SPHSX
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain Q； PDBConstruct 1–516； UniProt 1–516

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	4xtc
Deposition date deposition_date	2015-01-23
Structure title title	Crystal structure of bacterial alginate ABC transporter in complex with alginate pentasaccharide-bound periplasmic protein
Keywords keywords	ABC, alginate, sphingomonas, transporter, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

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.

4xtc__assembly_1__model_1

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

Download this curve (.dat)

4xtc__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4xtc__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	47.77 Å
Rg (electron density)	47.40 Å
Total Rg	47.42 Å
Atom count	14264
Residues	1793
Excluded volume	256590 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4xtc__assembly_1__model_1`	pentameric （5）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	AlgM1
Molecular weight formula_weight	34286.6 kDa
Mutation mutation	2-24 deletion mutant
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	M
Atom count atom_count	14264

MERLWKDIKRDWLLYAMLLPTIIWFLIFLYKPMIGLQMAFKQYSAWKGIAGSPWIGFDHFVTLFQSEQFIRAIKNTLTLSGLSLLFGFPMPILLALMINEVYSKGYRKAVQTIVYLPHFISIVIVAGLVVTFLSPSTGVVNNMLSWIGLDRVYFLTQPEWFRPIYISSNIWKEAGFDSIVYLAAIMSINPALYESAQVDGATRWQMITRITLPCIVPTIAVLLVIRLGHILEVGFEYIILLYQPTTYETADVISTYIYRLGLQGARYDIATAAGIFNAVVALVIVLFANHMSRRITKTGVF

Source Source

Source organism organism	Sphingomonas sp. A1
NCBI taxonomy ID ncbi_taxonomy_id	90322
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	AlgM2
Molecular weight formula_weight	34496.6 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	N

MLATPFYSRSDRIFGIVNAVLLGIFALCALYPIIYIFSMSISSGAAVTQGRVFLLPVDIDFSAYGRVLHDKLFWTSYANTIFYTVFGVVTSLIFIVPGAYALSKPRIRGRRVFGFIIAFTMWFNAGMIPFFLNMRDLGLLDNRFGILIGFACNAFNIILMRNYFESISASFEEAARMDGANDLQILWKVYIPLAKPALATITLLCAISRWNGYFWAMVLLRAEEKIPLQVYLKKTIVDLNVNEEFAGALLTNSYSMETVVGAIIVMSIIPVIIVYPVVQKYFTKGVMLGGVKELEHHHHHHHHHH

Source Source

Source organism organism	Sphingomonas sp. A1
NCBI taxonomy ID ncbi_taxonomy_id	90322
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	AlgS
Molecular weight formula_weight	39574.5 kDa
Mutation mutation	E160Q
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	S,T

MVASVSIQNVVKRYDKTTVVHGVSLDIEPGEFVVLVGPSGCGKSTTLRMVAGLEEISGGTIRIDGRVINDLAPKDRDVAMVFQNYALYPHLNVRDNISFGLRLKRTKKSVIDAAVKTAADILGLQPLLERKPSDLSGGQRQRVAMGRAIVRDPKVFLFDQPLSNLDAKLRTQMRAEIKRLHQRLGTTVIYVTHDQVEAMTLADRIVVMRDGLIEQIGKPMDLFLHPANTFVASFIGSPPMNLMPARIAVDSTQHVELNGGNRISLLPRAGTHLAPGQEVVFGIRPEDVTLDGVEGSERAQIKATVDIVEPLGSESILHATVGDHSLVVKVGGLNEVHPGDPVTLHVDLTRVHLFDAQSQASIY

Source Source

Source organism organism	Sphingomonas sp. A1
NCBI taxonomy ID ncbi_taxonomy_id	90322
Host organism host_organism	Escherichia coli

Entity 4 Entity 4 polymer

Description description	AlgQ2
Molecular weight formula_weight	59688.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Q

MKKMMLSVAAVATLMAFAAPVATAKEATWVTDKPLTLKIHMHFRDKWVWDENWPVAKESFRLTNVKLQSVANKAATNSQEQFNLMMASGDLPDVVGGDNLKDKFIQYGQEGAFVPLNKLIDQYAPHIKAFFKSHPEVERAIKAPDGNIYFIPYVPDGVVARGYFIREDWLKKLNLKPPQNIDELYTVLKAFKEKDPNGNGKADEVPFIDRHPDEVFRLVNFWGARSSGSDNYMDFYIDNGRVKHPWAETAFRDGMKHVAQWYKEGLIDKEIFTRKARAREQMFGGNLGGFTHDWFASTMTFNEGLAKTVPGFKLIPIAPPTNSKGQRWEEDSRQKVRPDGWAITVKNKNPVETIKFFDFYFSRPGRDISNFGVPGVTYDIKNGKAVFKDSVLKSPQPVNNQLYDMGAQIPIGFWQDYDYERQWTTPEAQAGIDMYVKGKYVMPGFEGVNMTREERAIYDKYWADVRTYMYEMGQAWVMGTKDVDKTWDEYQRQLKLRGLYQVLQMMQQAYDRQYKN

Source Source

Source organism organism	Sphingomonas sp. A1
NCBI taxonomy ID ncbi_taxonomy_id	90322
Host organism host_organism	Escherichia coli

Entity 5 Entity 5 branched

Description description	;beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid-(1-4)-beta-D-mannopyranuronic acid ;
Molecular weight formula_weight	898.6 kDa
Source method src_method	man
Copy count entity_count	1

▼

6. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id	4xtcM01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	3720 — MetI-like fold
Homologous superfamily homologous superfamily	10 — MetI-like

Domain ID domain_id	4xtcN00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	3720 — MetI-like fold
Homologous superfamily homologous superfamily	10 — MetI-like

Domain ID domain_id	4xtcQ01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	4xtcQ02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

Domain ID domain_id	4xtcS01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	4xtcS02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	100 — RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain

Domain ID domain_id	4xtcS03
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

Domain ID domain_id	4xtcT01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	4xtcT02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	100 — RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain

Domain ID domain_id	4xtcT03
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	140 — Nucleic acid-binding proteins

▶

Unit-cell length a length_a	71.608 Å
Unit-cell length b length_b	132.963 Å
Unit-cell length c length_c	272.973 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	3.600 Å
Low-resolution limit resolution_low	37.420 Å
R factor r_factor	0.2410
R_work r_work	0.2384
R_free r_free	0.2885

Crystal structure of bacterial alginate ABC transporter in complex with alginate pentasaccharide-bound periplasmic protein

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

AlgM1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

AlgM2

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

AlgS

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

AlgQ2

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

4xtc__assembly_1__model_1

4xtc__assembly_1__model_1 | I(q)

4xtc__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 branched

6. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

7. Citations (1)