SAXSdb — 1pkn

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

PYRUVATE KINASE

Oryctolagus cuniculus

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 1–530	Not recorded	K POTASSIUM ION × 1 MN MANGANESE (II) ION × 1 PYR PYRUVIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.90 Å

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 1PKN	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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state Different ligand/ion 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 mutation/modification Different oligomeric state Different ligand/ion 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 mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 oligomeric state 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 oligomeric state 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
2G50 The location of the allosteric amino acid binding site of muscle pyruvate kinase. Deposited 2006-02-22	Different construct Different mutation/modification Different oligomeric state 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 mutation/modification Different oligomeric state 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 construct Different mutation/modification Different oligomeric state 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 construct Different mutation/modification Different oligomeric state 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 construct Different mutation/modification Different oligomeric state 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 construct Different mutation/modification Different oligomeric state 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 construct Different mutation/modification Different oligomeric state 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 construct Different mutation/modification Different oligomeric state 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
8F6M Complex of Rabbit muscle pyruvate kinase with ADP and the phosphonate analogue of PEP mimicking the Michaelis complex. Deposited 2022-11-16	Different construct Different mutation/modification Different oligomeric state 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 construct Different mutation/modification Different oligomeric state 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 1–530； UniProt 1–530

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	1pkn
Deposition date deposition_date	1994-03-25
Structure title title	STRUCTURE OF RABBIT MUSCLE PYRUVATE KINASE COMPLEXED WITH MN2+, K+, AND PYRUVATE
Keywords keywords	PHOSPHOTRANSFERASE; PHOSPHOTRANSFERASE
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	25.15 Å
Radius of gyration Rg (electron density) rg_electron	24.56 Å
Forward intensity I(0) i0	53097400.00
Molecular weight molecular_weight	56295.0 kDa
Excluded volume excluded_volume	70496 Å³
Envelope volume envelope_volume	87069 Å³
Hydration-shell volume shell_volume	29620 Å³
Envelope diameter envelope_diameter	86.7 Å
Shell Rg shell_rg	31.98 Å
Envelope Rg envelope_rg	24.96 Å
Shape Rg shape_rg	24.57 Å
Total Rg total_rg	25.35 Å
Total atoms total_atoms	3937
Residues n_residues	514
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	87.7 Å
Rg (real space) rg_real	25.16 Å
Rg uncertainty (real space) rg_real_error	0.55 Å
I(0) (real space) i0_real	5.3100e+07
I(0) uncertainty (real space) i0_real_error	6.6700e+05
Rg (reciprocal space) rg_reciprocal	25.16 Å
I(0) (reciprocal space) i0_reciprocal	53100000.0000
Solution quality estimate total_estimate	0.6487
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	29.2 Å
Skewness Skewness skewness	0.450
Kurtosis Kurtosis kurtosis	-0.064
Angular range angular_range	— – 0.3150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	14940000.0000
Real-space data points n_real_points	64
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.707; Stabil: 1.000; Sysdev: 0.120; Positv: 1.000; Valcen: 0.952; Smooth: 0.995

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	PYRUVATE KINASE
Molecular weight formula_weight	57797.5 kDa
EC 编号 ec_number	2.7.1.40
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	3937

SKSHSEAGSAFIQTQQLHAAMADTFLEHMCRLDIDSAPITARNTGIICTIGPASRSVETLKEMIKSGMNVARMNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMAACDENILWLDYKNICKVVEVGSKVYVDDGLISLQVKQKGPDFLVTEVENGGFLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVDEDVDMVFASFIRKAADVHEVRKILGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMIIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEAAMFHRKLFEELARSSSHSTDLMEAMAMGSVEASYKCLAAALIVLTESGRSAHQVARYRPRAPIIAVTRNHQTARQAHLYRGIFPVVCKDPVQEAWAEDVDLRVNLAMNVGKAAGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP

来源 Source

来源生物 organism	Oryctolagus cuniculus
通用名 common_name	rabbit
NCBI Class编号 ncbi_taxonomy_id	9986

Entity 2 Entity 2 non-polymer

Description description	POTASSIUM ION
Molecular weight formula_weight	39.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	MANGANESE (II) ION
Molecular weight formula_weight	54.9 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	PYRUVIC ACID
Molecular weight formula_weight	88.1 kDa
Source method src_method	syn
Copy count entity_count	1

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1pkna1
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	d1pkna2
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	d1pkna3
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 (3 domains)

Domain ID domain_id	1pknA01
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	1pknA02
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	1pknA03
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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8. Citations (1)

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Unit-cell length a length_a	83.600 Å
Unit-cell length b length_b	109.900 Å
Unit-cell length c length_c	146.800 Å
Unit-cell angle α angle_alpha	94.90 °
Unit-cell angle β angle_beta	93.60 °
Unit-cell angle γ angle_gamma	112.30 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	2.900 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.1910
R_work r_work	—
R_free r_free	—

fit	/app/data/saxs_computation/pk/1pkn/1pkn.fit
pddf	/app/data/pr_computation/pk/1pkn/1pkn.pr.out
profile	/app/data/saxs_computation/pk/1pkn/1pkn.dat

STRUCTURE OF RABBIT MUSCLE PYRUVATE KINASE COMPLEXED WITH MN2+, K+, AND PYRUVATE