1BU6: Protein

Crystal structures of escherichia coli glycerol kinase and the mutant A65T in an inactive tetramer: conformational changes and implications for allosteric regulation. Determined by X-ray diffraction at 2.37 Å resolution. Released 16 Sept 1998.

Method: X-ray diffraction
Resolution: 2.37 Å
Organism: Escherichia coli
Chains: 4
Atoms: 15,815
Mol. weight: 225.71 kDa
Released: 16 Sept 1998

Explore 1BU6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1BU6 contains 85 α-helices and 114 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 O: 19 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	5-11	7	1
β-strand	15-21	7	1
β-strand	27-34	8	1
β-strand	38	1	2
β-strand	46-47	2	2
α-helix	49-67	19
α-helix	71-73	3
β-strand	74-81	8	1
β-strand	86-90	5	2
β-strand	95-101	7	2
α-helix	109-117	9
α-helix	121-127	7
α-helix	137-147	11
α-helix	151-157	7
β-strand	161-163	3	2
α-helix	165-173	9
β-strand	180-181	2	3
α-helix	183-186	4
β-strand	192-193	2	4
β-strand	198-199	2	4
α-helix	201-207	7
β-strand	216-217	2	3
β-strand	221-227	7	1
β-strand	237-241	5	1
β-strand	243-244	2	1
α-helix	245-252	8
β-strand	260-265	6	5
β-strand	269-276	8	5
β-strand	287-292	6	5
β-strand	298-306	9	5
α-helix	310-314	5
α-helix	315-319	5
α-helix	328-333	6
β-strand	343-345	3	6
β-strand	348	1	7
β-strand	350	1	7
β-strand	352	1	5
β-strand	362-367	6	6
α-helix	373-399	27
β-strand	405-409	5	5
α-helix	411-414	4
α-helix	416-426	11
β-strand	429-432	4	5
α-helix	438-450	13
α-helix	457-461	5
β-strand	468-470	3	5
α-helix	476-493	18

Chain X: 19 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	5-11	7	22
β-strand	15-22	8	22
β-strand	27-34	8	22
β-strand	38	1	23
β-strand	46-47	2	23
α-helix	49-67	19
α-helix	71-73	3
β-strand	74-81	8	22
β-strand	86-90	5	23
β-strand	95-96	2	23
β-strand	100-101	2	23
α-helix	109-117	9
α-helix	121-128	8
α-helix	137-147	11
α-helix	151-156	6
β-strand	160-164	5	23
α-helix	165-173	9
β-strand	180-182	3	24
α-helix	183-187	5
β-strand	192-193	2	25
β-strand	198-199	2	25
α-helix	201-206	6
α-helix	211-213	3
β-strand	216-218	3	24
β-strand	225-227	3	22
β-strand	237-244	8	22
α-helix	245-252	8
β-strand	261-265	5	26
β-strand	269-274	6	26
β-strand	287-292	6	26
β-strand	298-306	9	26
α-helix	310-318	9
α-helix	328-333	6
β-strand	343-345	3	20
β-strand	348	1	27
β-strand	350	1	27
β-strand	352	1	26
β-strand	362-367	6	20
α-helix	373-399	27
β-strand	405-407	3	28
β-strand	408-409	2	26
α-helix	411-414	4
α-helix	416-426	11
β-strand	429-433	5	28
α-helix	438-449	12
α-helix	457-460	4
β-strand	466-470	5	28
α-helix	476-493	18

Chain Y: 23 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	5-11	7	8
β-strand	15-22	8	8
β-strand	27-34	8	8
β-strand	38	1	9
β-strand	46-47	2	9
α-helix	49-67	19
α-helix	71-73	3
β-strand	74-81	8	8
β-strand	86	1	9
β-strand	87-90	4	10
β-strand	96	1	10
α-helix	99	1
β-strand	100-101	2	9
α-helix	102	1
α-helix	109-117	9
α-helix	121-128	8
α-helix	137-147	11
α-helix	151-156	6
β-strand	160-163	4	10
α-helix	165-173	9
β-strand	180-182	3	11
α-helix	183-186	4
β-strand	192-193	2	12
β-strand	198-199	2	12
α-helix	201-207	7
α-helix	211-213	3
β-strand	216-218	3	11
β-strand	221-227	7	8
β-strand	237-244	8	8
α-helix	245-252	8
β-strand	260-265	6	13
β-strand	269-274	6	13
α-helix	280-282	3
β-strand	287-292	6	13
β-strand	298-306	9	13
α-helix	310-314	5
α-helix	315-320	6
α-helix	328-333	6
β-strand	343-345	3	6
β-strand	348	1	14
β-strand	350	1	14
β-strand	362-367	6	6
α-helix	373-399	27
β-strand	405-409	5	13
α-helix	411-414	4
α-helix	416-426	11
β-strand	429-432	4	13
α-helix	438-449	12
α-helix	457-460	4
β-strand	468-470	3	13
α-helix	476-493	18

Chain Z: 24 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	5-11	7	15
β-strand	15-22	8	15
β-strand	27-34	8	15
β-strand	38	1	16
β-strand	46-47	2	16
α-helix	49-67	19
α-helix	71-73	3
β-strand	74-81	8	15
β-strand	86-90	5	16
β-strand	96	1	16
α-helix	99	1
β-strand	100-101	2	16
α-helix	102	1
α-helix	109-117	9
α-helix	121-123	3
α-helix	124-128	5
α-helix	137-147	11
α-helix	152-156	5
β-strand	160-164	5	16
α-helix	165-173	9
β-strand	180-182	3	17
α-helix	183-186	4
β-strand	192-193	2	18
β-strand	198-199	2	18
α-helix	201-206	6
α-helix	211-213	3
β-strand	216-218	3	17
β-strand	225-227	3	15
β-strand	237-239	3	15
β-strand	243-244	2	15
α-helix	245-251	7
β-strand	261-265	5	19
β-strand	269-274	6	19
α-helix	280-282	3
β-strand	287-292	6	19
β-strand	298-306	9	19
α-helix	310-314	5
α-helix	315-319	5
α-helix	328-333	6
β-strand	343-345	3	20
β-strand	348	1	21
β-strand	350	1	21
β-strand	352	1	19
β-strand	362-367	6	20
α-helix	373-399	27
β-strand	405-410	6	19
α-helix	411-414	4
α-helix	416-426	11
β-strand	429-433	5	19
α-helix	438-450	13
α-helix	457-460	4
β-strand	466-470	5	19
α-helix	476-493	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (glycerol kinase)	O, X, Y, Z	protein	501	Escherichia coli	P0A6F3 (AlphaFold model)

Sequence of entity 1 (O, X, Y, Z), FASTA

>1BU6_1 PROTEIN (GLYCEROL KINASE) (chains O, X, Y, Z)
TEKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPMEIWATQSSTL
VEVLTKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAIVWQCRRTAEICEHLKRDGL
EDYIRSNTGLVIDPYFSGTKVKWILDHVEGSRERARRGELLFGTVDTWLIWKMTQGRVHV
TDYTNASRTMLFNIHTLDWDDKMLEVLDIPREMLPEVRRSSEVYGQTNIGGKGGTRIPIS
GIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNY
ALEGAVFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLGAPYWDPYA
RGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQ
FQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTERN
YRYAGWKKAVKRAMAWEEHDE

Primary citation

Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation. Feese, M.D., Faber, H.R., Bystrom, C.E. et al. Structure (1998) 6:1407-1418. DOI 10.1016/S0969-2126(98)00140-3 · PubMed

Other PDB entries of the same protein (UniProt P0A6F3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3EZW 2.0 Å, Crystal Structure of a Hyperactive Escherichia coli Glycerol Kinase Mutant Gly230 -->…
1GLA 2.6 Å, Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase
1GLB 2.6 Å, Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase
1GLF 2.62 Å, Crystal structures of escherichia coli glycerol kinase and the mutant A65T in an…
1GLC 2.65 Å, Cation promoted association (CPA) of a regulatory and target protein is controlled by…
1GLD 2.93 Å, Cation promoted association (CPA) of a regulatory and target protein is controlled by…
1GLE 2.94 Å, Cation promoted association (CPA) of a regulatory and target protein is controlled by…
1BWF 3.0 Å, Escherichia coli glycerol kinase mutant with bound ATP analog showing substantial domain…
1GLJ 3.0 Å, Escherichia coli glycerol kinase mutant with bound ATP analog showing substantial domain…
1GLL 3.0 Å, Escherichia coli glycerol kinase mutant with bound ATP analog showing substantial domain…
1BOT 3.05 Å, Crystal structure of the complex between escherichia coli glycerol kinase and the…
1BO5 3.2 Å, Crystal structure of the complex between escherichia coli glycerol kinase and the…

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