SAXSdb — 8f5u

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

Pyruvate kinase PKM

OrganismNot specified

UniProt P11974

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–531 Chain B； UniProt 1–531 Chain C； UniProt 1–531 Chain D； UniProt 1–531	Not recorded	GOL GLYCEROL × 8 EDO 1,2-ETHANEDIOL × 2 K POTASSIUM ION × 8 MG MAGNESIUM ION × 4 PYR PYRUVIC ACID × 2 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.8；282 K；50 mM Tris 50 mM NaCl and a range of 7.5 to 10% PEG 20,000	Resolution 2.30 Å R-free 0.220

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 8F5U	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A49 BIS MG-ATP-K-OXALATE COMPLEX OF PYRUVATE KINASE Deposited 1998-02-12	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–530（530 aa） Chain B 1–530（530 aa） Chain C 1–530（530 aa） Chain D 1–530（530 aa）	Not recorded	K POTASSIUM ION × 4 OXL OXALATE ION × 4 MG MAGNESIUM ION × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；pH 6.0	Resolution 2.10 Å
1A49 BIS MG-ATP-K-OXALATE COMPLEX OF PYRUVATE KINASE Deposited 1998-02-12	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain E 1–530（530 aa） Chain F 1–530（530 aa） Chain G 1–530（530 aa） Chain H 1–530（530 aa）	Not recorded	K POTASSIUM ION × 4 OXL OXALATE ION × 4 MG MAGNESIUM ION × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；pH 6.0	Resolution 2.10 Å
1A5U PYRUVATE KINASE COMPLEX WITH BIS MG-ATP-NA-OXALATE Deposited 1998-02-18	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–530（530 aa） Chain B 1–530（530 aa） Chain C 1–530（530 aa） Chain D 1–530（530 aa）	Not recorded	NA SODIUM ION × 4 OXL OXALATE ION × 4 MG MAGNESIUM ION × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；pH 6.0	Resolution 2.35 Å
1A5U PYRUVATE KINASE COMPLEX WITH BIS MG-ATP-NA-OXALATE Deposited 1998-02-18	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain E 1–530（530 aa） Chain F 1–530（530 aa） Chain G 1–530（530 aa） Chain H 1–530（530 aa）	Not recorded	NA SODIUM ION × 4 OXL OXALATE ION × 4 MG MAGNESIUM ION × 7 ATP ADENOSINE-5'-TRIPHOSPHATE × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；pH 6.0	Resolution 2.35 Å
1AQF PYRUVATE KINASE FROM RABBIT MUSCLE WITH MG, K, AND L-PHOSPHOLACTATE Deposited 1997-07-29	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–530（530 aa） Chain B 1–530（530 aa） Chain C 1–530（530 aa） Chain D 1–530（530 aa）	Not recorded	K POTASSIUM ION × 4 MG MAGNESIUM ION × 4 PEQ L-PHOSPHOLACTATE × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.70 Å
1AQF PYRUVATE KINASE FROM RABBIT MUSCLE WITH MG, K, AND L-PHOSPHOLACTATE Deposited 1997-07-29	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain E 1–530（530 aa） Chain F 1–530（530 aa） Chain G 1–530（530 aa） Chain H 1–530（530 aa）	Not recorded	K POTASSIUM ION × 4 MG MAGNESIUM ION × 4 PEQ L-PHOSPHOLACTATE × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.70 Å
1F3W RECOMBINANT RABBIT MUSCLE PYRUVATE KINASE Deposited 2000-06-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–530（530 aa） Chain B 1–530（530 aa） Chain C 1–530（530 aa） Chain D 1–530（530 aa）	Not recorded	K POTASSIUM ION × 4 MN MANGANESE (II) ION × 4 PYR PYRUVIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；291 K；PEG 8000, manganese chloride, potassium chloride, sodium pyruvate, succinate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.00 Å R-free 0.257
1F3W RECOMBINANT RABBIT MUSCLE PYRUVATE KINASE Deposited 2000-06-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain E 1–530（530 aa） Chain F 1–530（530 aa） Chain G 1–530（530 aa） Chain H 1–530（530 aa）	Not recorded	K POTASSIUM ION × 4 MN MANGANESE (II) ION × 4 PYR PYRUVIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；291 K；PEG 8000, manganese chloride, potassium chloride, sodium pyruvate, succinate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 3.00 Å R-free 0.257
1F3X S402P MUTANT OF RABBIT MUSCLE PYRUVATE KINASE Deposited 2000-06-06	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–530（530 aa） Chain B 1–530（530 aa） Chain C 1–530（530 aa） Chain D 1–530（530 aa）	Mutation：S402P Mutation：S402P Mutation：S402P Mutation：S402P	K POTASSIUM ION × 4 MN MANGANESE (II) ION × 4 PYR PYRUVIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；291 K；PEG 8000, manganese chloride, potassium chloride, sodium pyruvate, succinate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.80 Å R-free 0.270
1F3X S402P MUTANT OF RABBIT MUSCLE PYRUVATE KINASE Deposited 2000-06-06	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain E 1–530（530 aa） Chain F 1–530（530 aa） Chain G 1–530（530 aa） Chain H 1–530（530 aa）	Mutation：S402P Mutation：S402P Mutation：S402P Mutation：S402P	K POTASSIUM ION × 4 MN MANGANESE (II) ION × 4 PYR PYRUVIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；291 K；PEG 8000, manganese chloride, potassium chloride, sodium pyruvate, succinate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.80 Å R-free 0.270
1PKN STRUCTURE OF RABBIT MUSCLE PYRUVATE KINASE COMPLEXED WITH MN2+, K+, AND PYRUVATE Deposited 1994-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–530（530 aa）	Not recorded	K POTASSIUM ION × 1 MN MANGANESE (II) ION × 1 PYR PYRUVIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.90 Å
2G50 The location of the allosteric amino acid binding site of muscle pyruvate kinase. Deposited 2006-02-22	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–530（530 aa） Chain B 1–530（530 aa） Chain C 1–530（530 aa） Chain D 1–530（530 aa）	Not recorded	MN MANGANESE (II) ION × 4 K POTASSIUM ION × 4 NA SODIUM ION × 6 ALA ALANINE × 4 PYR PYRUVIC ACID × 4 EDO 1,2-ETHANEDIOL × 13 GOL GLYCEROL × 12 ETE 2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；60 mM Succinate (pH 5.5), 5.8 mM sodium pyruvate, 2.4 mM MnCl2, 450 mM KCl, and a range of 18 to 20% PEG 8000, 150 mM Alanine, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.65 Å R-free 0.174
2G50 The location of the allosteric amino acid binding site of muscle pyruvate kinase. Deposited 2006-02-22	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain E 1–530（530 aa） Chain F 1–530（530 aa） Chain G 1–530（530 aa） Chain H 1–530（530 aa）	Not recorded	MN MANGANESE (II) ION × 4 K POTASSIUM ION × 4 NA SODIUM ION × 6 ALA ALANINE × 4 PYR PYRUVIC ACID × 4 EDO 1,2-ETHANEDIOL × 16 GOL GLYCEROL × 16	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；60 mM Succinate (pH 5.5), 5.8 mM sodium pyruvate, 2.4 mM MnCl2, 450 mM KCl, and a range of 18 to 20% PEG 8000, 150 mM Alanine, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.65 Å R-free 0.174
3N25 The structure of muscle pyruvate kinase in complex with proline, pyruvate, and Mn2+ Deposited 2010-05-17	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–531（531 aa） Chain B 1–531（531 aa） Chain C 1–531（531 aa） Chain D 1–531（531 aa）	Not recorded	PRO PROLINE × 4 MN MANGANESE (II) ION × 4 PYR PYRUVIC ACID × 4 K POTASSIUM ION × 4 NA SODIUM ION × 6 GOL GLYCEROL × 11 EDO 1,2-ETHANEDIOL × 9	X-RAY DIFFRACTION X-ray crystallization conditions hanging drop vapor diffusion；pH 5.5；298 K；60 mM Succinate (pH 5.5), 5.8 mM sodium pyruvate, 2.4 mM MnCl2, 450 mM KCl, 444 mM Proline and a range of 18 to 20% PEG 8000., hanging drop vapor diffusion, temperature 298K	Resolution 2.41 Å R-free 0.268
3N25 The structure of muscle pyruvate kinase in complex with proline, pyruvate, and Mn2+ Deposited 2010-05-17	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain E 1–531（531 aa） Chain F 1–531（531 aa） Chain G 1–531（531 aa） Chain H 1–531（531 aa）	Not recorded	PRO PROLINE × 4 MN MANGANESE (II) ION × 4 PYR PYRUVIC ACID × 4 K POTASSIUM ION × 4 NA SODIUM ION × 6 GOL GLYCEROL × 8 EDO 1,2-ETHANEDIOL × 6	X-RAY DIFFRACTION X-ray crystallization conditions hanging drop vapor diffusion；pH 5.5；298 K；60 mM Succinate (pH 5.5), 5.8 mM sodium pyruvate, 2.4 mM MnCl2, 450 mM KCl, 444 mM Proline and a range of 18 to 20% PEG 8000., hanging drop vapor diffusion, temperature 298K	Resolution 2.41 Å R-free 0.268
7R6Y E117K mutant pyruvate kinase from rabbit muscle Deposited 2021-06-24	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–531（531 aa） Chain B 1–531（531 aa） Chain C 1–531（531 aa） Chain D 1–531（531 aa）	Mutation：E117K Mutation：E117K Mutation：E117K Mutation：E117K	ACT ACETATE ION × 9 OXL OXALATE ION × 4 MG MAGNESIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；291.15 K；0.2 M magnesium acetate, 0.1 M sodium cacodylate pH 6.5, and 18% w/v Polyethylene Glycol 8000	Resolution 2.25 Å R-free 0.250
8F5T Rabbit muscle pyruvate kinase in complex with sodium and magnesium Deposited 2022-11-15	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–531（531 aa） Chain B 1–531（531 aa） Chain C 1–531（531 aa） Chain D 1–531（531 aa）	Not recorded	MG MAGNESIUM ION × 4 NA SODIUM ION × 4 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；50 mM Tris 50 mM NaCl and a range of 7.5 to 10% PEG 20,000	Resolution 2.41 Å R-free 0.232
8F5T Rabbit muscle pyruvate kinase in complex with sodium and magnesium Deposited 2022-11-15	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain E 1–531（531 aa） Chain F 1–531（531 aa） Chain G 1–531（531 aa） Chain H 1–531（531 aa）	Not recorded	MG MAGNESIUM ION × 4 NA SODIUM ION × 4 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 4 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；50 mM Tris 50 mM NaCl and a range of 7.5 to 10% PEG 20,000	Resolution 2.41 Å R-free 0.232
8F6M Complex of Rabbit muscle pyruvate kinase with ADP and the phosphonate analogue of PEP mimicking the Michaelis complex. Deposited 2022-11-16	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–531（531 aa） Chain F 1–531（531 aa） Chain G 1–531（531 aa） Chain H 1–531（531 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 2 SIN SUCCINIC ACID × 5 MN MANGANESE (II) ION × 7 K POTASSIUM ION × 4 ALA ALANINE × 4 GOL GLYCEROL × 13 GZ3 (E)-2-METHYL-3-PHOSPHONOACRYLATE × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；15 mM succinate, 50 mM KCl, 19 to 24% PEG 8,000 well solution	Resolution 2.15 Å R-free 0.205
8F6M Complex of Rabbit muscle pyruvate kinase with ADP and the phosphonate analogue of PEP mimicking the Michaelis complex. Deposited 2022-11-16	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain B 1–531（531 aa） Chain C 1–531（531 aa） Chain D 1–531（531 aa） Chain E 1–531（531 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 3 SIN SUCCINIC ACID × 7 MN MANGANESE (II) ION × 8 K POTASSIUM ION × 4 ALA ALANINE × 4 GOL GLYCEROL × 13 GZ3 (E)-2-METHYL-3-PHOSPHONOACRYLATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；15 mM succinate, 50 mM KCl, 19 to 24% PEG 8,000 well solution	Resolution 2.15 Å R-free 0.205

11 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	KPYM_RABIT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–531； UniProt 1–531 Author chain B； PDBConstruct 1–531； UniProt 1–531 Author chain C； PDBConstruct 1–531； UniProt 1–531 Author chain D； PDBConstruct 1–531； UniProt 1–531

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	8f5u
Deposition date deposition_date	2022-11-15
Structure title title	Rabbit muscle pyruvate kinase in complex with magnesium, potassium and pyruvate
Keywords keywords	glycolysis, metabolic kinase, central metabolism, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	40.93 Å
Radius of gyration Rg (electron density) rg_electron	40.80 Å
Forward intensity I(0) i0	770216000.00
Molecular weight molecular_weight	228760.0 kDa
Excluded volume excluded_volume	286780 Å³
Envelope volume envelope_volume	362620 Å³
Hydration-shell volume shell_volume	70918 Å³
Envelope diameter envelope_diameter	142.6 Å
Shell Rg shell_rg	48.58 Å
Envelope Rg envelope_rg	40.97 Å
Shape Rg shape_rg	40.82 Å
Total Rg total_rg	41.09 Å
Total atoms total_atoms	16013
Residues n_residues	2072
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	135.4 Å
Rg (real space) rg_real	40.85 Å
Rg uncertainty (real space) rg_real_error	0.90 Å
I(0) (real space) i0_real	7.7020e+08
I(0) uncertainty (real space) i0_real_error	1.3140e+07
Rg (reciprocal space) rg_reciprocal	40.93 Å
I(0) (reciprocal space) i0_reciprocal	770300000.0000
Solution quality estimate total_estimate	0.8919
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	48.6 Å
Skewness Skewness skewness	0.254
Kurtosis Kurtosis kurtosis	-0.468
Angular range angular_range	— – 0.1950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	251900000.0000
Real-space data points n_real_points	40
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.885; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.937

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (8)

Entity 1 Entity 1 polymer

Description description	Pyruvate kinase PKM
Molecular weight formula_weight	58114.0 kDa
EC 编号 ec_number	2.7.1.40,2.7.11.1,2.7.10.2
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	17110

MSKSHSEAGSAFIQTQQLHAAMADTFLEHMCRLDIDSAPITARNTGIICTIGPASRSVETLKEMIKSGMNVARMNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVDVGSKVYVDDGLISLQVKQKGPDFLVTEVENGGFLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKAADVHEVRKILGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMIIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEAAMFHRKLFEELARASSHSTDLMEAMAMGSVEASYKCLAAALIVLTESGRSAHQVARYRPRAPIIAVTRNHQTARQAHLYRGIFPVVCKDPVQEAWAEDVDLRVNLAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP

Entity 2 Entity 2 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 3 Entity 3 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	POTASSIUM ION
Molecular weight formula_weight	39.1 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 5 Entity 5 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 6 Entity 6 non-polymer

Description description	PYRUVIC ACID
Molecular weight formula_weight	88.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 7 Entity 7 non-polymer

Description description	2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
Molecular weight formula_weight	122.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 8 Entity 8 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1051

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7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id	8f5uA01
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	8f5uA02
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	8f5uB01
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	8f5uB02
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	8f5uC01
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	8f5uD01
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

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8. Citations (1)

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Unit-cell length a length_a	113.131 Å
Unit-cell length b length_b	130.198 Å
Unit-cell length c length_c	170.282 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	2.300 Å
Low-resolution limit resolution_low	47.270 Å
R factor r_factor	0.1667
R_work r_work	0.1638
R_free r_free	0.2202

fit	/app/data/saxs_computation/f5/8f5u/8f5u.fit
pddf	/app/data/pr_computation/f5/8f5u/8f5u.pr.out
profile	/app/data/saxs_computation/f5/8f5u/8f5u.dat

Rabbit muscle pyruvate kinase in complex with magnesium, potassium and pyruvate