1e0u

Structure R271L mutant of E. coli pyruvate kinase

Method: X-RAY DIFFRACTION

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

Pyruvate kinase

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	SULFATE ION × 4 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A0A0G552_ECOLX
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–470； UniProt 73–542 Author chain B； PDBConstruct 1–470； UniProt 73–542 Author chain C； PDBConstruct 1–470； UniProt 73–542 Author chain D； PDBConstruct 1–470； UniProt 73–542

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	1e0u
Deposition date deposition_date	2000-04-10
Structure title title	Structure R271L mutant of E. coli pyruvate kinase
Keywords keywords	PHOSPHOTRANSFERASE, GLYCOLYSIS, ALLOSTERY; PHOSPHOTRANSFERASE
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.

1e0u__assembly_1__model_1

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

Download this curve (.dat)

1e0u__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1e0u__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	44.58 Å
Rg (electron density)	44.11 Å
Total Rg	44.30 Å
Atom count	13800
Residues	1844
Excluded volume	247300 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1e0u__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 (3)

Entity 1 Entity 1 polymer

Description description	Pyruvate kinase
Molecular weight formula_weight	50751.4 kDa
EC 编号 ec_number	2.7.1.40
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	14000

MKKTKIVCTIGPKTESEEMLAKMLDAGMNVMRLNFSHGDYAEHGQRIQNLRNVMSKTGKTAAILLDTKGPEIRTMKLEGGNDVSLKAGQTFTFTTDKSVIGNSEMVAVTYEGFTTDLSVGNTVLVDDGLIGMEVTAIEGNKVICKVLNNGDLGENKGVNLPGVSIALPALAEKDKQDLIFGCEQGVDFVAASFIRKRSDVIEIREHLKAHGGENIHIISKIENQEGLNNFDEILEASDGIMVARGDLGVEIPVEEVIFAQKMMIEKCIRALKVVITATMMLDSMIKNPRPTRAEAGDVANAILDGTDAVMLSGESAKGKYPLEAVSIMATICERTDRVMNSRLEFNNDNRKLRITEAVCRGAVETAEKLDAPLIVVATQGGKSARAVRKYFPDATILALTTNEKTAHQLVLSKGVVPQLVKEITSTDDFYRLGKELALQSGLAHKGDVVVMVSGALVPSGTTNTASVHVL

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	200

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6. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

Domain ID domain_id	d1e0ua1
Class class	b — All beta proteins
Fold Fold fold	b.58 — PK beta-barrel domain-like
Superfamily Superfamily superfamily	b.58.1 — PK beta-barrel domain-like
Family Family family	b.58.1.1 — Pyruvate kinase beta-barrel domain

Domain ID domain_id	d1e0ua2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.12 — Phosphoenolpyruvate/pyruvate domain
Family Family family	c.1.12.1 — Pyruvate kinase

Domain ID domain_id	d1e0ua3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.49 — Pyruvate kinase C-terminal domain-like
Superfamily Superfamily superfamily	c.49.1 — PK C-terminal domain-like
Family Family family	c.49.1.1 — Pyruvate kinase, C-terminal domain

Domain ID domain_id	d1e0ub1
Class class	b — All beta proteins
Fold Fold fold	b.58 — PK beta-barrel domain-like
Superfamily Superfamily superfamily	b.58.1 — PK beta-barrel domain-like
Family Family family	b.58.1.1 — Pyruvate kinase beta-barrel domain

Domain ID domain_id	d1e0ub2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.12 — Phosphoenolpyruvate/pyruvate domain
Family Family family	c.1.12.1 — Pyruvate kinase

Domain ID domain_id	d1e0ub3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.49 — Pyruvate kinase C-terminal domain-like
Superfamily Superfamily superfamily	c.49.1 — PK C-terminal domain-like
Family Family family	c.49.1.1 — Pyruvate kinase, C-terminal domain

Domain ID domain_id	d1e0uc1
Class class	b — All beta proteins
Fold Fold fold	b.58 — PK beta-barrel domain-like
Superfamily Superfamily superfamily	b.58.1 — PK beta-barrel domain-like
Family Family family	b.58.1.1 — Pyruvate kinase beta-barrel domain

Domain ID domain_id	d1e0uc2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.12 — Phosphoenolpyruvate/pyruvate domain
Family Family family	c.1.12.1 — Pyruvate kinase

Domain ID domain_id	d1e0uc3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.49 — Pyruvate kinase C-terminal domain-like
Superfamily Superfamily superfamily	c.49.1 — PK C-terminal domain-like
Family Family family	c.49.1.1 — Pyruvate kinase, C-terminal domain

Domain ID domain_id	d1e0ud1
Class class	b — All beta proteins
Fold Fold fold	b.58 — PK beta-barrel domain-like
Superfamily Superfamily superfamily	b.58.1 — PK beta-barrel domain-like
Family Family family	b.58.1.1 — Pyruvate kinase beta-barrel domain

Domain ID domain_id	d1e0ud2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.12 — Phosphoenolpyruvate/pyruvate domain
Family Family family	c.1.12.1 — Pyruvate kinase

Domain ID domain_id	d1e0ud3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.49 — Pyruvate kinase C-terminal domain-like
Superfamily Superfamily superfamily	c.49.1 — PK C-terminal domain-like
Family Family family	c.49.1.1 — Pyruvate kinase, C-terminal domain

CATH v4.4 (12 domains)

Domain ID domain_id	1e0uA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1380 — Pyruvate Kinase; Chain: A, domain 1
Homologous superfamily homologous superfamily	20 — Pyruvate kinase, C-terminal domain

Domain ID domain_id	1e0uA02
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	60 — Phosphoenolpyruvate-binding domains

Domain ID domain_id	1e0uA03
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	33 — M1 Pyruvate Kinase; Domain 3
Homologous superfamily homologous superfamily	10 — PK beta-barrel domain-like

Domain ID domain_id	1e0uB01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1380 — Pyruvate Kinase; Chain: A, domain 1
Homologous superfamily homologous superfamily	20 — Pyruvate kinase, C-terminal domain

Domain ID domain_id	1e0uB02
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	60 — Phosphoenolpyruvate-binding domains

Domain ID domain_id	1e0uB03
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	33 — M1 Pyruvate Kinase; Domain 3
Homologous superfamily homologous superfamily	10 — PK beta-barrel domain-like

Domain ID domain_id	1e0uC01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1380 — Pyruvate Kinase; Chain: A, domain 1
Homologous superfamily homologous superfamily	20 — Pyruvate kinase, C-terminal domain

Domain ID domain_id	1e0uC02
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	60 — Phosphoenolpyruvate-binding domains

Domain ID domain_id	1e0uC03
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	33 — M1 Pyruvate Kinase; Domain 3
Homologous superfamily homologous superfamily	10 — PK beta-barrel domain-like

Domain ID domain_id	1e0uD01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1380 — Pyruvate Kinase; Chain: A, domain 1
Homologous superfamily homologous superfamily	20 — Pyruvate kinase, C-terminal domain

Domain ID domain_id	1e0uD02
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	60 — Phosphoenolpyruvate-binding domains

Domain ID domain_id	1e0uD03
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	33 — M1 Pyruvate Kinase; Domain 3
Homologous superfamily homologous superfamily	10 — PK beta-barrel domain-like

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Unit-cell length a length_a	74.010 Å
Unit-cell length b length_b	129.590 Å
Unit-cell length c length_c	241.770 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	16

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	15.000 Å
R factor r_factor	0.2450
R_work r_work	0.2450
R_free r_free	0.3120

Structure R271L mutant of E. coli pyruvate kinase

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

Pyruvate kinase

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

1e0u__assembly_1__model_1

1e0u__assembly_1__model_1 | I(q)

1e0u__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

CATH v4.4 (12 domains)

7. Citations (1)

Structure R271L mutant of E. coli pyruvate kinase

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

Pyruvate kinase

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

1e0u__assembly_1__model_1

1e0u__assembly_1__model_1 | I(q)

1e0u__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (12 domains)

CATH v4.4 (12 domains)

7. Citations (1)