6PFK: Phosphofructokinase, inhibited T-state

Phosphofructokinase, inhibited T-state. Determined by X-ray diffraction at 2.6 Å resolution. Released 11 Jul 1996.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Geobacillus stearothermophilus
Chains: 4
Atoms: 9,681
Mol. weight: 137.3 kDa
Ligands: PGA
Released: 11 Jul 1996

Explore 6PFK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6PFK contains 60 α-helices and 60 β-strands across 4 chains. 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: 14 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	1
α-helix	16-29	14
β-strand	33-37	5	1
α-helix	40-46	7
β-strand	49-52	4	1
α-helix	54-57	4
β-strand	70	1	2
α-helix	75-77	3
α-helix	79-92	14
β-strand	96-101	6	1
α-helix	103-114	12
β-strand	119-123	5	1
β-strand	124	1	3
β-strand	137	1	3
α-helix	139-155	17
β-strand	158	1	4
β-strand	163-168	6	5
α-helix	175-183	9
β-strand	188-190	3	5
α-helix	198-211	14
β-strand	216-221	6	5
α-helix	227-238	12
β-strand	242-246	5	5
α-helix	248-252	5
α-helix	258-276	19
β-strand	282-287	6	1
β-strand	290-295	6	1
α-helix	296-301	6
α-helix	309-318	10

Chain B: 16 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	6
α-helix	16-29	14
β-strand	33-37	5	6
α-helix	40-45	6
β-strand	49-51	3	6
α-helix	54-57	4
β-strand	70	1	7
α-helix	75-77	3
α-helix	79-92	14
β-strand	96-101	6	6
α-helix	103-114	12
β-strand	119-123	5	6
β-strand	124-125	2	8
β-strand	137-138	2	8
α-helix	139-155	17
β-strand	158	1	9
β-strand	163-168	6	10
α-helix	175-184	10
β-strand	188-190	3	10
α-helix	198-211	14
β-strand	216-221	6	10
α-helix	222-224	3
α-helix	227-238	12
β-strand	242-246	5	10
α-helix	248-252	5
α-helix	258-276	19
β-strand	282-287	6	6
β-strand	290-295	6	6
α-helix	296-300	5
α-helix	304-305	2
α-helix	309-318	10

Chain C: 15 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	3-8	6	11
α-helix	16-30	15
β-strand	33-37	5	11
α-helix	40-46	7
β-strand	49-52	4	11
α-helix	54-57	4
β-strand	70	1	9
α-helix	75-77	3
α-helix	79-92	14
β-strand	97-101	5	11
α-helix	103-114	12
β-strand	119-123	5	11
β-strand	124-125	2	12
β-strand	137-138	2	12
α-helix	139-155	17
β-strand	158	1	7
β-strand	163-168	6	10
α-helix	175-183	9
β-strand	188-190	3	10
α-helix	198-211	14
β-strand	216-221	6	10
α-helix	222-224	3
α-helix	227-238	12
β-strand	242-246	5	10
α-helix	248-252	5
α-helix	258-277	20
β-strand	282-287	6	11
β-strand	290-295	6	11
α-helix	296-300	5
α-helix	309-318	10

Chain D: 15 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	13
α-helix	16-29	14
β-strand	33-37	5	13
α-helix	40-46	7
β-strand	49-52	4	13
α-helix	54-57	4
β-strand	70	1	4
α-helix	74-76	3
α-helix	79-91	13
β-strand	96-101	6	13
α-helix	103-113	11
β-strand	119-123	5	13
β-strand	124-125	2	14
β-strand	137-138	2	14
α-helix	139-155	17
β-strand	158	1	2
β-strand	163-168	6	5
α-helix	175-184	10
β-strand	188-190	3	5
α-helix	198-210	13
β-strand	216-221	6	5
α-helix	227-238	12
β-strand	242-246	5	5
α-helix	248-250	3
α-helix	258-276	19
β-strand	282-287	6	13
β-strand	290-295	6	13
α-helix	296-301	6
α-helix	304-305	2
α-helix	309-318	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Phosphofructokinase	A, B, C, D	protein	319	Geobacillus stearothermophilus	P00512 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>6PFK_1 PHOSPHOFRUCTOKINASE (chains A, B, C, D)
MKRIGVLTSGGDSPGMNAAIRSVVRKAIYHGVEVYGVYHGYAGLIAGNIKKLEVGDVGDI
IHRGGTILYTARCPEFKTEEGQKKGIEQLKKHGIEGLVVIGGDGSYQGAKKLTEHGFPCV
GVPGTIDNDIPGTDFTIGFDTALNTVIDAIDKIRDTATSHERTYVIEVMGRHAGDIALWS
GLAGGAETILIPEADYDMNDVIARLKRGHERGKKHSIIIVAEGVGSGVDFGRQIQEATGF
ETRVTVLGHVQRGGSPTAFDRVLASRLGARAVELLLEGKGGRCVGIQNNQLVDHDIAEAL
ANKHTIDQRMYALSKELSI

Ligands and cofactors

ID	Name	Formula	Copies
PGA	2-phosphoglycolic acid	C2 H5 O6 P	4

Primary citation

Structural basis of the allosteric behaviour of phosphofructokinase. Schirmer, T., Evans, P.R. Nature (1990) 343:140-145. DOI 10.1038/343140a0 · PubMed

Other PDB entries of the same protein (UniProt P00512 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4I7E 2.0 Å, Crystal Structure of the Bacillus stearothermophilus Phosphofructokinase Mutant D12A in…
4I36 2.3 Å, Crystal Structure of the Bacillus stearothermophilus Phosphofructokinase Mutant D12A
3PFK 2.4 Å, Phosphofructokinase. Structure and control
4PFK 2.4 Å, Phosphofructokinase. Structure and control
4I4I 2.49 Å, Crystal Structure of Bacillus stearothermophilus Phosphofructokinase mutant T156A bound…
3U39 2.79 Å, Crystal Structure of the apo Bacillus Stearothermophilus phosphofructokinase
1MTO 3.2 Å, Crystal structure of a Phosphofructokinase mutant from Bacillus stearothermophilus bound…

Browse structure collections

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