1MTO: 6-phosphofructokinase

Crystal structure of a Phosphofructokinase mutant from Bacillus stearothermophilus bound with fructose-6-phosphate. Determined by X-ray diffraction at 3.2 Å resolution. Released 31 Dec 2002.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: Geobacillus stearothermophilus
Chains: 8
Atoms: 19,328
Mol. weight: 275.42 kDa
Ligands: F6P
Released: 31 Dec 2002

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

Secondary structure: helices and β-sheets

1MTO contains 108 α-helices and 114 β-strands across 8 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: 13 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	1
α-helix	16-28	13
β-strand	33-37	5	1
α-helix	41-46	6
β-strand	49-51	3	1
α-helix	83-90	8
β-strand	96-101	6	1
α-helix	103-113	11
β-strand	119-123	5	1
β-strand	124	1	2
β-strand	137	1	2
α-helix	139-159	21
β-strand	163-168	6	3
α-helix	175-183	9
β-strand	188-190	3	3
α-helix	198-211	14
β-strand	216-221	6	3
α-helix	222-224	3
α-helix	227-238	12
β-strand	242-246	5	3
α-helix	248-251	4
α-helix	258-277	20
β-strand	281-287	7	1
β-strand	290-295	6	1
α-helix	296-300	5
α-helix	308-317	10

Chain B: 14 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	4
α-helix	16-29	14
β-strand	33-37	5	4
α-helix	40-46	7
β-strand	49-51	3	4
α-helix	54-57	4
α-helix	79-91	13
β-strand	97-101	5	4
α-helix	103-114	12
β-strand	119-123	5	4
β-strand	124	1	5
β-strand	137	1	5
α-helix	139-159	21
β-strand	163-167	5	6
α-helix	175-184	10
β-strand	188-190	3	6
α-helix	200-210	11
β-strand	216-220	5	6
α-helix	222-224	3
α-helix	227-237	11
β-strand	242-246	5	6
α-helix	249-252	4
α-helix	258-276	19
β-strand	282-286	5	4
β-strand	291-295	5	4
α-helix	296-301	6
α-helix	308-316	9

Chain C: 12 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	7
α-helix	16-29	14
β-strand	33-37	5	7
α-helix	40-46	7
β-strand	49-52	4	7
α-helix	75-77	3
α-helix	79-91	13
β-strand	96-101	6	7
α-helix	103-114	12
β-strand	120-123	4	7
β-strand	124	1	8
β-strand	135	1	7
β-strand	137	1	8
α-helix	139-159	21
β-strand	163-168	6	9
α-helix	175-184	10
β-strand	188-190	3	9
α-helix	198-208	11
β-strand	216-221	6	9
α-helix	227-237	11
β-strand	242-246	5	9
α-helix	249-251	3
α-helix	258-276	19
β-strand	282-287	6	7
β-strand	290-295	6	7
α-helix	308-316	9

Chain D: 14 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	10
α-helix	16-28	13
β-strand	33-37	5	10
α-helix	40-46	7
β-strand	49-51	3	10
α-helix	74-76	3
α-helix	79-89	11
β-strand	96-101	6	10
α-helix	103-114	12
β-strand	119-123	5	10
β-strand	124-125	2	11
β-strand	137-138	2	11
α-helix	139-159	21
β-strand	163-168	6	12
α-helix	175-184	10
β-strand	188-190	3	12
β-strand	191	1	13
β-strand	194	1	13
α-helix	198-208	11
β-strand	217-221	5	12
β-strand	223	1	14
β-strand	225	1	14
α-helix	227-238	12
β-strand	242-246	5	12
α-helix	248-251	4
α-helix	255-257	3
α-helix	258-276	19
β-strand	282-286	5	10
β-strand	291-295	5	10
α-helix	296-301	6
α-helix	308-316	9

Chain E: 13 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	15
α-helix	16-28	13
β-strand	33-37	5	15
α-helix	42-45	4
β-strand	49-51	3	15
α-helix	79-92	14
β-strand	96-101	6	15
α-helix	103-114	12
β-strand	119-123	5	15
β-strand	124	1	16
β-strand	137	1	16
α-helix	139-160	22
β-strand	163-168	6	17
α-helix	175-184	10
β-strand	188-190	3	17
α-helix	198-209	12
β-strand	216-221	6	17
α-helix	227-238	12
β-strand	242-246	5	17
α-helix	248-252	5
α-helix	255-257	3
α-helix	258-274	17
β-strand	282-286	5	15
β-strand	291-294	4	15
α-helix	296-301	6
α-helix	308-316	9

Chain F: 15 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	18
α-helix	16-29	14
β-strand	33-36	4	18
β-strand	51-52	2	18
α-helix	54-57	4
α-helix	74-77	4
α-helix	79-88	10
β-strand	96-101	6	18
α-helix	103-111	9
β-strand	119-123	5	18
β-strand	124	1	19
β-strand	137	1	19
α-helix	139-160	22
β-strand	163-168	6	20
α-helix	175-183	9
β-strand	188-190	3	20
α-helix	198-207	10
β-strand	216-221	6	20
α-helix	227-238	12
β-strand	242-246	5	20
α-helix	248-252	5
α-helix	255-257	3
α-helix	258-276	19
β-strand	282-287	6	18
β-strand	290-295	6	18
α-helix	296-299	4
α-helix	303-304	2
α-helix	308-318	11

Chain G: 13 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	21
α-helix	16-29	14
β-strand	33-37	5	21
α-helix	40-46	7
β-strand	49	1	21
β-strand	52	1	21
α-helix	80-92	13
β-strand	96-101	6	21
α-helix	103-113	11
β-strand	119-123	5	21
β-strand	124	1	22
β-strand	135	1	21
β-strand	137	1	22
α-helix	139-158	20
β-strand	163-168	6	23
α-helix	175-184	10
β-strand	188-190	3	23
α-helix	198-207	10
β-strand	216-221	6	23
α-helix	222-224	3
α-helix	227-235	9
β-strand	242-245	4	23
α-helix	248-252	5
α-helix	258-276	19
β-strand	282-286	5	21
β-strand	291-295	5	21
α-helix	296-300	5
α-helix	308-316	9

Chain H: 14 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	24
α-helix	16-29	14
β-strand	33-37	5	24
α-helix	38	1
α-helix	40-45	6
β-strand	49-51	3	24
α-helix	74-77	4
α-helix	80-90	11
β-strand	97-101	5	24
α-helix	103-114	12
β-strand	119-123	5	24
β-strand	124	1	25
β-strand	135	1	26
β-strand	137	1	25
α-helix	139-160	22
β-strand	163-168	6	27
α-helix	175-182	8
β-strand	188-190	3	27
α-helix	198-208	11
β-strand	216-221	6	27
α-helix	227-238	12
β-strand	242-246	5	27
α-helix	248-251	4
α-helix	258-276	19
β-strand	282-283	2	24
β-strand	286-287	2	26
β-strand	290-291	2	26
β-strand	294-295	2	24
α-helix	296-300	5
α-helix	308-316	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
6-phosphofructokinase	A, B, C, D, E, F, G, H	protein	319	Geobacillus stearothermophilus	P00512 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA

>1MTO_1 6-phosphofructokinase (chains A, B, C, D, E, F, G, H)
MKRIGVLTSGGDSPGMNAAIRSVVRKAIYHGVEVYGVYHGYAGLIAGNIKKLEVGDVGDI
IHRGGTILYTARCPEFKTEEGQKKGIEQLKKHGIEGLVVIGGDGSYQGAKKLTEHGFPCV
GVPGTIDNDIPGTDFTIGFDTALNTVIDAIDKIRDTATSHERTWVIEVMGRHAGDIALYS
GLAGGAETILIPEADYDMNDVIARLKRGHERGKKHSIIIVAEGVGSGVDFGRQIQEATGF
ETRVTVLGHVQRGGSPTAFDRVLASRLGARAVELLLEGKGGRCVGIQNNQLVDHDIAEAL
ANKHTIDQRMYALSKELSI

Ligands and cofactors

ID	Name	Formula	Copies
F6P	6-O-phosphono-beta-D-fructofuranose	C6 H13 O9 P	8

Primary citation

Reversible Ligand-Induced Dissociation of a Tryptophan-Shift Mutant of Phosphofructokinase from Bacillus stearothermophilus. Riley-Lovingshimer, M.R., Ronning, D.R., Sacchettini, J.C. et al. Biochemistry (2002) 41:12967-12974. DOI 10.1021/bi0263412 · 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…
6PFK 2.6 Å, Phosphofructokinase, inhibited T-state
3U39 2.79 Å, Crystal Structure of the apo Bacillus Stearothermophilus phosphofructokinase

Browse structure collections

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