8f6m

Complex of Rabbit muscle pyruvate kinase with ADP and the phosphonate analogue of PEP mimicking the Michaelis complex.

Method: X-RAY DIFFRACTION D_max: 177.2 Å Quality: GOOD

▼

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 F； UniProt 1–531 Chain G； UniProt 1–531 Chain H； UniProt 1–531	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
2	Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain B； UniProt 1–531 Chain C； UniProt 1–531 Chain D； UniProt 1–531 Chain E； UniProt 1–531	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

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 8F6M	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
8F5U Rabbit muscle pyruvate kinase in complex with magnesium, potassium and pyruvate 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	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

11 other PDB entries and 19 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 Author chain E； PDBConstruct 1–531； UniProt 1–531 Author chain F； PDBConstruct 1–531； UniProt 1–531 Author chain G； PDBConstruct 1–531； UniProt 1–531 Author chain H； 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.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	8f6m
Deposition date deposition_date	2022-11-16
Structure title title	Complex of Rabbit muscle pyruvate kinase with ADP and the phosphonate analogue of PEP mimicking the Michaelis complex.
Keywords keywords	glycolysis, metabolic kinase, central metabolism, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

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

Radius of gyration Rg (Guinier) rg_guinier	54.52 Å
Radius of gyration Rg (electron density) rg_electron	54.32 Å
Forward intensity I(0) i0	3077230000.00
Molecular weight molecular_weight	461940.0 kDa
Excluded volume excluded_volume	576920 Å³
Envelope volume envelope_volume	785840 Å³
Hydration-shell volume shell_volume	114830 Å³
Envelope diameter envelope_diameter	189.6 Å
Shell Rg shell_rg	63.76 Å
Envelope Rg envelope_rg	52.58 Å
Shape Rg shape_rg	54.34 Å
Total Rg total_rg	54.48 Å
Total atoms total_atoms	32315
Residues n_residues	4141
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

▼

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

Maximum dimension Dmax dmax	177.2 Å
Rg (real space) rg_real	54.30 Å
Rg uncertainty (real space) rg_real_error	1.45 Å
I(0) (real space) i0_real	3.0770e+09
I(0) uncertainty (real space) i0_real_error	6.3140e+07
Rg (reciprocal space) rg_reciprocal	54.68 Å
I(0) (reciprocal space) i0_reciprocal	3079000000.0000
Solution quality estimate total_estimate	0.8855
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	73.3 Å
Skewness Skewness skewness	0.109
Kurtosis Kurtosis kurtosis	-0.483
Angular range angular_range	— – 0.1450 Å⁻¹
Current regularization parameter α current_alpha	0.0001
Highest regularization parameter α highest_alpha	221800000.0000
Real-space data points n_real_points	30
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: 0.979; Smooth: 0.874

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (9)

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	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H
Atom count atom_count	35355

MSKSHSEAGSAFIQTQQLHAAMADTFLEHMCRLDIDSAPITARNTGIICTIGPASRSVETLKEMIKSGMNVARMNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVDVGSKVYVDDGLISLQVKQKGPDFLVTEVENGGFLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKAADVHEVRKILGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMIIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEAAMFHRKLFEELARASSHSTDLMEAMAMGSVEASYKCLAAALIVLTESGRSAHQVARYRPRAPIIAVTRNHQTARQAHLYRGIFPVVCKDPVQEAWAEDVDLRVNLAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP

Entity 2 Entity 2 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 3 Entity 3 non-polymer

Description description	SUCCINIC ACID
Molecular weight formula_weight	118.1 kDa
Source method src_method	syn
Copy count entity_count	12

Entity 4 Entity 4 non-polymer

Description description	MANGANESE (II) ION
Molecular weight formula_weight	54.9 kDa
Source method src_method	nat
Copy count entity_count	15

Entity 5 Entity 5 non-polymer

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

Entity 6 Entity 6 non-polymer

Description description	ALANINE
Molecular weight formula_weight	89.1 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 7 Entity 7 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	26

Entity 8 Entity 8 non-polymer

Description description	(E)-2-METHYL-3-PHOSPHONOACRYLATE
Molecular weight formula_weight	166.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 9 Entity 9 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	2882

▶

8. Citations (1)

▶

Unit-cell length a length_a	93.026 Å
Unit-cell length b length_b	216.396 Å
Unit-cell length c length_c	258.151 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	32

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

Resolution resolution	2.150 Å
Low-resolution limit resolution_low	46.020 Å
R factor r_factor	0.1584
R_work r_work	0.1559
R_free r_free	0.2047

fit	/app/data/saxs_computation/f6/8f6m/8f6m.fit
pddf	/app/data/pr_computation/f6/8f6m/8f6m.pr.out
profile	/app/data/saxs_computation/f6/8f6m/8f6m.dat