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3n25

The structure of muscle pyruvate kinase in complex with proline, pyruvate, and Mn2+

Method: X-RAY DIFFRACTION Dmax: 195.0 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Pyruvate kinase isozymes M1/M2

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

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 3N25 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
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
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 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

SAXS profile for 3n25

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3n25
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3n25
Deposition date deposition_date2010-05-17
Structure title titleThe structure of muscle pyruvate kinase in complex with proline, pyruvate, and Mn2+
Keywords keywordspyruvate kinase, glycolysis, allosteric regulation, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier56.58 Å
Radius of gyration Rg (electron density) rg_electron56.79 Å
Forward intensity I(0) i02958700000.00
Molecular weight molecular_weight457590.0 kDa
Excluded volume excluded_volume573710 ų
Envelope volume envelope_volume771870 ų
Hydration-shell volume shell_volume111780 ų
Envelope diameter envelope_diameter198.9 Å
Shell Rg shell_rg60.04 Å
Envelope Rg envelope_rg56.20 Å
Shape Rg shape_rg56.80 Å
Total Rg total_rg56.84 Å
Total atoms total_atoms31991
Residues n_residues4125
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax195.0 Å
Rg (real space) rg_real56.63 Å
Rg uncertainty (real space) rg_real_error1.75 Å
I(0) (real space) i0_real2.9590e+09
I(0) uncertainty (real space) i0_real_error5.4140e+07
Rg (reciprocal space) rg_reciprocal56.51 Å
I(0) (reciprocal space) i0_reciprocal2958000000.0000
Solution quality estimate total_estimate0.8791
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.7 Å
Skewness Skewness skewness0.323
Kurtosis Kurtosis kurtosis-0.519
Angular range angular_range— – 0.1400 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha254100000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.850; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.878
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (9)

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7. Fold Classification (SCOP + CATH) 24 domains

CATH v4.4 (24 domains)

Domain ID domain_id3n25A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1380 — Pyruvate Kinase; Chain: A, domain 1
Homologous superfamily homologous superfamily20 — Pyruvate kinase, C-terminal domain
Domain ID domain_id3n25A02
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily60 — Phosphoenolpyruvate-binding domains
Domain ID domain_id3n25A03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology33 — M1 Pyruvate Kinase; Domain 3
Homologous superfamily homologous superfamily10 — PK beta-barrel domain-like
Domain ID domain_id3n25B01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1380 — Pyruvate Kinase; Chain: A, domain 1
Homologous superfamily homologous superfamily20 — Pyruvate kinase, C-terminal domain
Domain ID domain_id3n25B02
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily60 — Phosphoenolpyruvate-binding domains
Domain ID domain_id3n25B03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology33 — M1 Pyruvate Kinase; Domain 3
Homologous superfamily homologous superfamily10 — PK beta-barrel domain-like
Domain ID domain_id3n25C01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1380 — Pyruvate Kinase; Chain: A, domain 1
Homologous superfamily homologous superfamily20 — Pyruvate kinase, C-terminal domain
Domain ID domain_id3n25C02
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily60 — Phosphoenolpyruvate-binding domains
Domain ID domain_id3n25C03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology33 — M1 Pyruvate Kinase; Domain 3
Homologous superfamily homologous superfamily10 — PK beta-barrel domain-like
Domain ID domain_id3n25D01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1380 — Pyruvate Kinase; Chain: A, domain 1
Homologous superfamily homologous superfamily20 — Pyruvate kinase, C-terminal domain
Domain ID domain_id3n25D02
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily60 — Phosphoenolpyruvate-binding domains
Domain ID domain_id3n25D03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology33 — M1 Pyruvate Kinase; Domain 3
Homologous superfamily homologous superfamily10 — PK beta-barrel domain-like
Domain ID domain_id3n25E01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1380 — Pyruvate Kinase; Chain: A, domain 1
Homologous superfamily homologous superfamily20 — Pyruvate kinase, C-terminal domain
Domain ID domain_id3n25E02
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily60 — Phosphoenolpyruvate-binding domains
Domain ID domain_id3n25E03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology33 — M1 Pyruvate Kinase; Domain 3
Homologous superfamily homologous superfamily10 — PK beta-barrel domain-like
Domain ID domain_id3n25F01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1380 — Pyruvate Kinase; Chain: A, domain 1
Homologous superfamily homologous superfamily20 — Pyruvate kinase, C-terminal domain
Domain ID domain_id3n25F02
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily60 — Phosphoenolpyruvate-binding domains
Domain ID domain_id3n25F03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology33 — M1 Pyruvate Kinase; Domain 3
Homologous superfamily homologous superfamily10 — PK beta-barrel domain-like
Domain ID domain_id3n25G01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1380 — Pyruvate Kinase; Chain: A, domain 1
Homologous superfamily homologous superfamily20 — Pyruvate kinase, C-terminal domain
Domain ID domain_id3n25G02
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily60 — Phosphoenolpyruvate-binding domains
Domain ID domain_id3n25G03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology33 — M1 Pyruvate Kinase; Domain 3
Homologous superfamily homologous superfamily10 — PK beta-barrel domain-like
Domain ID domain_id3n25H01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1380 — Pyruvate Kinase; Chain: A, domain 1
Homologous superfamily homologous superfamily20 — Pyruvate kinase, C-terminal domain
Domain ID domain_id3n25H02
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily60 — Phosphoenolpyruvate-binding domains
Domain ID domain_id3n25H03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology33 — M1 Pyruvate Kinase; Domain 3
Homologous superfamily homologous superfamily10 — PK beta-barrel domain-like
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8. Citations (1)

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9. Files and Curves (10)