SAXSdb — 5ahu

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

FARNESYL PYROPHOSPHATE SYNTHASE, PUTATIVE

TRYPANOSOMA BRUCEI

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	FARNESYL PYROPHOSPHATE SYNTHASE × 2 （Q86C09） [2-(1-heptyl-1H-imidazol-3-ium-3-yl)ethane-1,1-diyl]bis(phosphonate) × 2 MAGNESIUM ION × 6 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	C9ZSP7_TRYB9
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–63； UniProt 1–63 Author chain C； PDBConstruct 1–63； UniProt 1–63

FARNESYL PYROPHOSPHATE SYNTHASE

TRYPANOSOMA BRUCEI

UniProt Q86C09

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	FARNESYL PYROPHOSPHATE SYNTHASE, PUTATIVE × 2 （C9ZSP7） [2-(1-heptyl-1H-imidazol-3-ium-3-yl)ethane-1,1-diyl]bis(phosphonate) × 2 MAGNESIUM ION × 6 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q86C09_9TRYP
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–294； UniProt 74–367 Author chain D； PDBConstruct 1–294； UniProt 74–367

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	5ahu
Deposition date deposition_date	2015-02-09
Structure title title	T. Brucei Farnesyl Diphosphate Synthase Complexed with Bisphosphonate BPH-1326
Keywords keywords	TRANSFERASE; TRANSFERASE
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.

5ahu__assembly_1__model_1

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

Download this curve (.dat)

5ahu__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5ahu__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	27.29 Å
Rg (electron density)	26.34 Å
Total Rg	27.12 Å
Atom count	5758
Residues	714
Excluded volume	103030 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5ahu__assembly_1__model_1`	tetrameric （4）	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	FARNESYL PYROPHOSPHATE SYNTHASE, PUTATIVE
Molecular weight formula_weight	7506.9 kDa
EC 编号 ec_number	2.5.1.10
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	5930

MPMQMFMQVYDEIQMFLLEELELKFDMDPNRVRYLRKMMDTTCLGGKYNRGLTVIDVAESLLS

Source Source

Source organism organism	TRYPANOSOMA BRUCEI
NCBI taxonomy ID ncbi_taxonomy_id	5691
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	FARNESYL PYROPHOSPHATE SYNTHASE
Molecular weight formula_weight	33456.2 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D

DGARRKRVLHDACVCGWMIEFLQAHYLVEDDIMDNSVTRRGKPCWYRHPDVTVQCAINDGLLLKSWTHMMAMHFFADRPFLQDLLCRFNRVDYTTAVGQLYDVTSMFDSNKLDPDVSQPTTTDFAEFTLSNYKRIVKYKTAYYTYLLPLVMGLIVSEALPTVDMGVTEELAMLMGEYFQVQDDVMDCFTPPERLGKVGTDIQDAKCSWLAVTFLAKASSAQVAEFKANYGSGDSEKVATVRRLYEEADLQGDYVAYEAAVAEQVKELIEKLRLCSPGFAASVETLWGKTYKRQK

Source Source

Source organism organism	TRYPANOSOMA BRUCEI
NCBI taxonomy ID ncbi_taxonomy_id	5691
Host organism host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 non-polymer

Description description	[2-(1-heptyl-1H-imidazol-3-ium-3-yl)ethane-1,1-diyl]bis(phosphonate)
Molecular weight formula_weight	351.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	172

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6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id	5ahuB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	600 — Farnesyl Diphosphate Synthase
Homologous superfamily homologous superfamily	10 — Farnesyl Diphosphate Synthase

Domain ID domain_id	5ahuD00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	600 — Farnesyl Diphosphate Synthase
Homologous superfamily homologous superfamily	10 — Farnesyl Diphosphate Synthase

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Unit-cell length a length_a	63.010 Å
Unit-cell length b length_b	117.860 Å
Unit-cell length c length_c	123.724 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	95.80 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

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

Resolution resolution	2.690 Å
Low-resolution limit resolution_low	32.840 Å
R factor r_factor	0.1841
R_work r_work	0.1812
R_free r_free	0.2355

T. Brucei Farnesyl Diphosphate Synthase Complexed with Bisphosphonate BPH-1326

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

FARNESYL PYROPHOSPHATE SYNTHASE, PUTATIVE

State in the Current Structure

Other States of the Same Protein in the Database

FARNESYL PYROPHOSPHATE SYNTHASE

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

5ahu__assembly_1__model_1

5ahu__assembly_1__model_1 | I(q)

5ahu__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 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)

T. Brucei Farnesyl Diphosphate Synthase Complexed with Bisphosphonate BPH-1326

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

FARNESYL PYROPHOSPHATE SYNTHASE, PUTATIVE

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

FARNESYL PYROPHOSPHATE SYNTHASE

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

5ahu__assembly_1__model_1

5ahu__assembly_1__model_1 | I(q)

5ahu__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 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)