1PKN: Rabbit muscle pyruvate kinase

Structure of rabbit muscle pyruvate kinase complexed with MN2+, K+, and pyruvate. Determined by X-ray diffraction at 2.9 Å resolution. Released 26 Jan 1995.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Oryctolagus cuniculus
Chains: 1
Atoms: 3,937
Mol. weight: 57.98 kDa
Ligands: MN, PYR
Released: 26 Jan 1995

Explore 1PKN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1PKN contains 23 α-helices and 27 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 23 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	14	1	1
α-helix	17-20	4
α-helix	25-30	6
β-strand	37	1	1
β-strand	45-49	5	2
α-helix	57-66	10
β-strand	70-74	5	2
α-helix	80-94	15
α-helix	101-103	3
β-strand	108-112	5	2
β-strand	119	1	3
β-strand	133	1	4
β-strand	138-142	5	5
β-strand	155-157	3	5
β-strand	172-175	4	5
β-strand	180-188	9	5
β-strand	191-198	8	5
β-strand	201	1	4
β-strand	207	1	3
β-strand	208-209	2	5
α-helix	222-234	13
β-strand	238-241	4	2
α-helix	248-257	10
α-helix	259-263	5
β-strand	265-270	6	2
α-helix	273-277	5
α-helix	279-285	7
β-strand	288-292	5	2
α-helix	293-299	7
α-helix	302-304	3
α-helix	305-319	15
β-strand	323-326	4	2
α-helix	332-334	3
α-helix	341-352	12
β-strand	357-360	4	2
α-helix	370-387	18
α-helix	390-400	11
α-helix	401-403	3
α-helix	407-421	15
β-strand	427-429	3	6
α-helix	435-441	7
β-strand	449-451	3	6
β-strand	452-453	2	7
α-helix	456-462	7
β-strand	468	1	6
β-strand	471-472	2	7
α-helix	476-478	3
α-helix	481-499	19
β-strand	507-512	6	6
β-strand	523-528	6	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Pyruvate kinase	A	protein	530	Oryctolagus cuniculus	P11974 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1PKN_1 PYRUVATE KINASE (chains A)
SKSHSEAGSAFIQTQQLHAAMADTFLEHMCRLDIDSAPITARNTGIICTIGPASRSVETL
KEMIKSGMNVARMNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIRT
GLIKGSGTAEVELKKGATLKITLDNAYMAACDENILWLDYKNICKVVEVGSKVYVDDGLI
SLQVKQKGPDFLVTEVENGGFLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVDEDVDMVF
ASFIRKAADVHEVRKILGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEI
PAEKVFLAQKMIIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIML
SGETAKGDYPLEAVRMQHLIAREAEAAMFHRKLFEELARSSSHSTDLMEAMAMGSVEASY
KCLAAALIVLTESGRSAHQVARYRPRAPIIAVTRNHQTARQAHLYRGIFPVVCKDPVQEA
WAEDVDLRVNLAMNVGKAAGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP

Ligands and cofactors

ID	Name	Formula	Copies
MN	Manganese (II) ion	Mn	1
PYR	Pyruvic acid	C3 H4 O3	1

Water and common crystallization additives (K) are not listed.

Primary citation

Structure of rabbit muscle pyruvate kinase complexed with Mn2+, K+, and pyruvate. Larsen, T.M., Laughlin, L.T., Holden, H.M. et al. Biochemistry (1994) 33:6301-6309. DOI 10.1021/bi00186a033 · PubMed

Other PDB entries of the same protein (UniProt P11974 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2G50 1.65 Å, The location of the allosteric amino acid binding site of muscle pyruvate kinase.
1A49 2.1 Å, Bis MG-ATP-K-oxalate complex of pyruvate kinase
8F6M 2.15 Å, Complex of Rabbit muscle pyruvate kinase with ADP and the phosphonate analogue of PEP…
7R6Y 2.25 Å, E117K mutant pyruvate kinase from rabbit muscle
8F5U 2.3 Å, Rabbit muscle pyruvate kinase in complex with magnesium, potassium and pyruvate
1A5U 2.35 Å, Pyruvate kinase complex with bis MG-ATP-na-oxalate
3N25 2.41 Å, The structure of muscle pyruvate kinase in complex with proline, pyruvate, and Mn2+
8F5T 2.41 Å, Rabbit muscle pyruvate kinase in complex with sodium and magnesium
1AQF 2.7 Å, Pyruvate kinase from rabbit muscle with MG, K, and L-phospholactate
1F3X 2.8 Å, S402P mutant of rabbit muscle pyruvate kinase
1F3W 3.0 Å, Recombinant rabbit muscle pyruvate kinase

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1PKN is part of these collections:

Metabolism and cellular energy

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