1Z6R: Mlc from Escherichia coli

Crystal structure of Mlc from Escherichia coli. Determined by X-ray diffraction at 2.7 Å resolution. Released 14 Jun 2005.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Escherichia coli
Chains: 4
Atoms: 11,728
Mol. weight: 179.52 kDa
Ligands: ZN
Released: 14 Jun 2005

Explore 1Z6R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1Z6R contains 75 α-helices and 80 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: 18 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	13-26	14
α-helix	33-39	7
α-helix	44-57	14
β-strand	60-62	3	1
β-strand	78-80	3	1
β-strand	86-93	8	2
β-strand	96-103	8	2
β-strand	108-115	8	2
α-helix	124-138	15
α-helix	140-142	3
β-strand	146-153	8	2
β-strand	156-158	3	3
β-strand	163-166	4	3
β-strand	176	1	3
α-helix	178-186	9
β-strand	190-194	5	2
α-helix	195-206	12
β-strand	215-220	6	4
β-strand	224-230	7	4
β-strand	233-234	2	4
β-strand	243	1	4
α-helix	245-247	3
β-strand	249	1	5
β-strand	256	1	6
β-strand	262	1	6
β-strand	264	1	5
α-helix	266-269	4
α-helix	271-282	12
α-helix	289-291	3
α-helix	297-305	9
α-helix	309-333	25
β-strand	337-341	5	4
α-helix	343-347	5
α-helix	348-362	15
α-helix	365-368	4
β-strand	372-375	4	4
α-helix	386-393	8
α-helix	398-403	6

Chain B: 20 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	13-28	16
β-strand	31	1	7
α-helix	33-39	7
α-helix	44-57	14
β-strand	60-62	3	7
β-strand	78-80	3	7
β-strand	85-93	9	8
β-strand	96-103	8	8
β-strand	108-115	8	8
α-helix	124-138	15
α-helix	140-142	3
β-strand	145-153	9	8
β-strand	156-158	3	9
β-strand	163-166	4	9
β-strand	176	1	9
α-helix	178-186	9
β-strand	190-194	5	8
α-helix	195-205	11
β-strand	215-220	6	10
β-strand	224-230	7	10
β-strand	233-234	2	10
α-helix	245-247	3
β-strand	249	1	11
α-helix	255	1
β-strand	256	1	12
α-helix	257	1
β-strand	262	1	12
β-strand	264	1	11
α-helix	265-269	5
α-helix	271-284	14
α-helix	289-291	3
α-helix	297-306	10
α-helix	309-333	25
β-strand	337-341	5	10
α-helix	343-347	5
α-helix	348-362	15
α-helix	365-368	4
β-strand	372-375	4	10
α-helix	386-395	10
α-helix	398-403	6

Chain C: 19 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	13-27	15
β-strand	31	1	13
α-helix	33-40	8
α-helix	44-57	14
β-strand	60-62	3	13
β-strand	78-80	3	13
β-strand	85-93	9	14
β-strand	96-103	8	14
β-strand	108-115	8	14
α-helix	124-138	15
β-strand	145-153	9	14
β-strand	156-158	3	15
β-strand	163-166	4	15
β-strand	176	1	15
α-helix	178-186	9
β-strand	190-194	5	14
α-helix	195-205	11
β-strand	215-220	6	16
β-strand	224-230	7	16
β-strand	233-234	2	16
β-strand	243	1	16
α-helix	245-247	3
β-strand	249	1	17
α-helix	255	1
β-strand	256	1	18
α-helix	257	1
β-strand	262	1	18
β-strand	264	1	17
α-helix	266-269	4
α-helix	271-283	13
α-helix	289-292	4
α-helix	297-306	10
α-helix	309-333	25
β-strand	337-341	5	16
α-helix	343-347	5
α-helix	348-362	15
α-helix	365-368	4
β-strand	372-375	4	16
α-helix	386-396	11
α-helix	398-403	6

Chain D: 18 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	13-28	16
β-strand	31	1	19
α-helix	33-39	7
α-helix	44-56	13
β-strand	60-62	3	19
β-strand	78-80	3	19
β-strand	85-92	8	20
β-strand	96-103	8	20
β-strand	108-115	8	20
α-helix	124-138	15
α-helix	140-142	3
β-strand	145-153	9	20
β-strand	157-158	2	21
β-strand	163-164	2	21
β-strand	176-177	2	21
α-helix	178-186	9
β-strand	190-194	5	20
α-helix	195-205	11
β-strand	215-220	6	22
β-strand	224-230	7	22
β-strand	233-234	2	22
β-strand	243	1	22
α-helix	245-247	3
β-strand	249	1	23
β-strand	264	1	23
α-helix	265-269	5
α-helix	271-284	14
α-helix	289-291	3
α-helix	297-305	9
α-helix	309-333	25
β-strand	337-341	5	22
α-helix	343-347	5
α-helix	348-362	15
α-helix	365-368	4
β-strand	372-375	4	22
α-helix	386-395	10
α-helix	398-403	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mlc protein	A, B, C, D	protein	406	Escherichia coli	P50456 (AlphaFold model)

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

>1Z6R_1 Mlc protein (chains A, B, C, D)
MVAENQPGHIDQIKQTNAGAVYRLIDQLGPVSRIDLSRLAQLAPASITKIVHEMLEAHLV
QELEIKEAGNRGRPAVGLVVETEAWHYLSLRISRGEIFLALRDLSSKLVVEESQELALKD
DLPLLDRIISHIDQFFIRHQKKLERLTSIAITLPGIIDTENGIVHRMPFYEDVKEMPLGE
ALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSS
SLVEIGHTQVDPYGKRCYCGNHGCLETIASVDSILELAQLRLNQSMSSMLHGQPLTVDSL
CQAALRGDLLAKDIITGVGAHVGRILAIMVNLFNPQKILIGSPLSKAADILFPVISDSIR
QQALPAYSQHISVESTQFSNQGTMAGAALVKDAMYNGSLLIRLLQG

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	4

Primary citation

The crystal structure of Mlc, a global regulator of sugar metabolism in Escherichia coli. Schiefner, A., Gerber, K., Seitz, S. et al. J Biol Chem (2005) 280:29073-29079. DOI 10.1074/jbc.M504215200 · PubMed

Other PDB entries of the same protein (UniProt P50456 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9SRW 2.3 Å, Cryo-EM structure of the Mlc tetramer in complex with the anti-repressor MtfA
9SRU 2.47 Å, Cryo-EM structure of Mlc in complex with ptsG operator DNA
9SRT 2.74 Å, Cryo-EM structure of the Mlc tetramer
3BP8 2.85 Å, Crystal structure of Mlc/EIIB complex
9SRX 2.96 Å, Cryo-EM structure of the Mlc repressor in complex with the glucose-specific IICB…

Browse structure collections

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