1GLF: 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 2.62 Å resolution. Released 16 Oct 1998.

Method: X-ray diffraction
Resolution: 2.62 Å
Organism: Escherichia coli
Chains: 4
Atoms: 15,981
Mol. weight: 226.92 kDa
Ligands: PO4, ADP
Released: 16 Oct 1998

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

Secondary structure: helices and β-sheets

1GLF contains 88 α-helices and 121 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: 24 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	5-11	7	1
β-strand	15	1	2
β-strand	16-21	6	1
β-strand	29-31	3	1
β-strand	34	1	2
β-strand	38	1	3
β-strand	46-47	2	3
α-helix	49-67	19
α-helix	71-73	3
β-strand	74-81	8	1
β-strand	86	1	3
β-strand	87-90	4	4
β-strand	96	1	4
α-helix	99	1
β-strand	100-101	2	3
α-helix	102	1
α-helix	109-118	10
α-helix	121-123	3
α-helix	124-128	5
α-helix	137-147	11
α-helix	151-156	6
β-strand	160-163	4	4
α-helix	165-173	9
β-strand	180-182	3	5
α-helix	183-187	5
β-strand	192-193	2	6
β-strand	198-199	2	6
α-helix	201-203	3
α-helix	204-208	5
β-strand	216-218	3	5
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	7
β-strand	269-274	6	7
α-helix	280-282	3
β-strand	287-292	6	7
β-strand	298-306	9	7
α-helix	310-315	6
α-helix	316-320	5
α-helix	328-335	8
β-strand	343-345	3	8
β-strand	348	1	9
β-strand	350	1	9
β-strand	362-367	6	8
α-helix	373-398	26
β-strand	405-407	3	10
β-strand	408-409	2	7
α-helix	411-414	4
α-helix	416-426	11
β-strand	429-433	5	10
α-helix	438-450	13
α-helix	457-459	3
β-strand	466-469	4	10
α-helix	478-493	16

Chain X: 21 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	5-11	7	28
β-strand	15-21	7	28
β-strand	29-34	6	28
β-strand	37-38	2	29
β-strand	46-47	2	29
α-helix	49-67	19
α-helix	71-73	3
β-strand	74-81	8	28
β-strand	86	1	29
β-strand	87-90	4	30
β-strand	95-96	2	30
β-strand	100-101	2	29
α-helix	109-118	10
α-helix	121-127	7
α-helix	137-147	11
α-helix	151-156	6
β-strand	160-163	4	30
α-helix	165-173	9
β-strand	180-182	3	31
α-helix	183-187	5
β-strand	192	1	32
β-strand	199	1	32
α-helix	201-207	7
α-helix	211-213	3
β-strand	216-218	3	31
β-strand	225-227	3	28
β-strand	237-244	8	28
α-helix	245-251	7
β-strand	261-265	5	33
β-strand	269-274	6	33
α-helix	280-282	3
β-strand	287-292	6	33
β-strand	298-306	9	33
α-helix	310-317	8
α-helix	328-333	6
β-strand	343-346	4	26
β-strand	348	1	34
β-strand	350	1	34
β-strand	352	1	33
β-strand	362-367	6	26
α-helix	373-399	27
β-strand	405-407	3	35
β-strand	408-409	2	33
α-helix	411-414	4
α-helix	416-426	11
β-strand	429-433	5	35
α-helix	438-449	12
α-helix	461-463	3
β-strand	466-469	4	35
α-helix	476-493	18
α-helix	498-499	2

Chain Y: 21 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	5-11	7	11
β-strand	15-22	8	11
β-strand	27-34	8	11
β-strand	38	1	12
β-strand	46-47	2	12
α-helix	49-67	19
α-helix	71-73	3
β-strand	74-81	8	11
β-strand	86	1	12
β-strand	87-90	4	13
β-strand	95-96	2	13
β-strand	100-101	2	12
α-helix	109-117	9
α-helix	121-123	3
α-helix	124-128	5
α-helix	130-131	2
α-helix	137-147	11
α-helix	151-156	6
β-strand	160-163	4	13
α-helix	165-174	10
β-strand	180-182	3	14
α-helix	183-186	4
β-strand	192-193	2	15
β-strand	198-199	2	15
α-helix	201-207	7
α-helix	211-213	3
β-strand	216-218	3	14
β-strand	221	1	11
β-strand	239-244	6	11
α-helix	245-251	7
β-strand	261-265	5	16
β-strand	269-274	6	16
β-strand	287-289	3	16
β-strand	292	1	17
β-strand	298	1	17
β-strand	301-306	6	16
α-helix	310-318	9
α-helix	329-333	5
β-strand	343-346	4	8
β-strand	348	1	18
β-strand	350	1	18
β-strand	352	1	16
β-strand	362-367	6	8
α-helix	373-399	27
β-strand	405-407	3	19
β-strand	408-409	2	16
α-helix	411-414	4
α-helix	416-426	11
β-strand	429-433	5	19
α-helix	438-450	13
α-helix	457-459	3
β-strand	466-470	5	19
α-helix	476-493	18

Chain Z: 22 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	5-11	7	20
β-strand	15-21	7	20
β-strand	27-34	8	20
β-strand	38	1	21
β-strand	46-47	2	21
α-helix	49-67	19
α-helix	71-73	3
β-strand	74-81	8	20
β-strand	86-90	5	21
β-strand	96-101	6	21
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	21
α-helix	165-173	9
β-strand	180-182	3	22
α-helix	183-186	4
β-strand	192-193	2	23
β-strand	198-199	2	23
α-helix	201-206	6
β-strand	216-218	3	22
β-strand	221	1	20
β-strand	226-227	2	24
β-strand	237-238	2	24
β-strand	239-244	6	20
α-helix	245-252	8
β-strand	260-265	6	25
β-strand	269-274	6	25
α-helix	279-282	4
β-strand	287-292	6	25
β-strand	298-306	9	25
α-helix	310-314	5
α-helix	315-320	6
α-helix	329-333	5
β-strand	343-345	3	26
α-helix	347-349	3
β-strand	362-367	6	26
α-helix	373-399	27
β-strand	406-407	2	27
β-strand	408-410	3	25
α-helix	412-414	3
α-helix	416-426	11
β-strand	430-433	4	27
α-helix	438-450	13
α-helix	458-461	4
β-strand	466-469	4	27
α-helix	471-473	3
α-helix	479-493	15

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

>1GLF_1 PROTEIN (GLYCEROL KINASE) (chains O, X, Y, Z)
TEKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPMEIWATQSSTL
VEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAIVWQCRRTAEICEHLKRDGL
EDYIRSNTGLVIDPYFSGTKVKWILDHVEGSRERARRGELLFGTVDTWLIWKMTQGRVHV
TDYTNASRTMLFNIHTLDWDDKMLEVLDIPREMLPEVRRSSEVYGQTNIGGKGGTRIPIS
GIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNY
ALEGAVFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLGAPYWDPYA
RGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQ
FQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTERN
YRYAGWKKAVKRAMAWEEHDE

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	2
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	4

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

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 -->…
1BU6 2.37 Å, Crystal structures of escherichia coli glycerol kinase and the mutant A65T in an…
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
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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