1QPG: 3-phosphoglycerate kinase, mutation R65Q

3-phosphoglycerate kinase, mutation R65Q. Determined by X-ray diffraction at 2.4 Å resolution. Released 10 Jun 1996.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Saccharomyces cerevisiae
Chains: 1
Atoms: 3,271
Mol. weight: 45.36 kDa
Ligands: MG, ANP, 3PG
Released: 10 Jun 1996

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

Secondary structure: helices and β-sheets

1QPG contains 26 α-helices and 22 β-strands across 1 chain. 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: 26 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	1
β-strand	7	1	2
α-helix	8-10	3
β-strand	17-21	5	2
β-strand	28	1	3
β-strand	33	1	3
α-helix	37-50	14
β-strand	56-60	5	2
α-helix	72-74	3
α-helix	77-87	11
β-strand	92-94	3	2
α-helix	100-107	8
α-helix	109-110	2
β-strand	113-117	5	2
α-helix	120-122	3
α-helix	124-127	4
β-strand	129-132	4	4
β-strand	135-138	4	4
α-helix	139-140	2
α-helix	141-153	13
β-strand	157-160	4	2
α-helix	163-165	3
α-helix	171-174	4
β-strand	181-183	3	2
α-helix	185-198	14
β-strand	205-209	5	5
α-helix	215-217	3
α-helix	218-224	7
β-strand	230-233	4	5
α-helix	235-237	3
α-helix	238-245	8
α-helix	257-273	17
β-strand	276-278	3	5
β-strand	282-286	5	6
β-strand	297-299	3	6
β-strand	309-313	5	6
α-helix	315-325	11
β-strand	330-334	5	5
α-helix	343-345	3
α-helix	347-362	16
β-strand	365-368	4	5
α-helix	371-379	9
α-helix	383-385	3
β-strand	388-389	2	5
α-helix	394-400	7
α-helix	406-409	4
α-helix	412	1
β-strand	413	1	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
3-phosphoglycerate kinase	A	protein	415	Saccharomyces cerevisiae	P00560 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1QPG_1 3-PHOSPHOGLYCERATE KINASE (chains A)
SLSSKLSVQDLDLKDKRVFIRVDFNVPLDGKKITSNQRIVAALPTIKYVLEHHPRYVVLA
SHLGQPNGERNEKYSLAPVAKELQSLLGKDVTFLNDCVGPEVEAAVKASAPGSVILLENL
RYHIEEEGSRKVDGQKVKASKEDVQKFRHELSSLADVYINDAFGTAHRAHSSMVGFDLPQ
RAAGFLLEKELKYFGKALENPTRPFLAILGGAKVADKIQLIDNLLDKVDSIIIGGGMAFT
FKKVLENTEIGDSIFDKAGAEIVPKLMEKAKAKGVEVVLPVDFIIADAFSADANTKTVTD
KEGIPAGWQGLDNGPESRKLFAATVAKAKTIVWNGPPGVFEFEKFAAGTKALLDEVVKSS
AAGNTVIIGGGDTATVAKKYGVTDKISHVSTGGGASLELLEGKELPGVAFLSEKK

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	1
3PG	3-phosphoglyceric acid	C3 H7 O7 P	1

Primary citation

Structure of the R65Q mutant of yeast 3-phosphoglycerate kinase complexed with Mg-AMP-PNP and 3-phospho-D-glycerate. McPhillips, T.M., Hsu, B.T., Sherman, M.A. et al. Biochemistry (1996) 35:4118-4127. DOI 10.1021/bi952500o · PubMed

Other PDB entries of the same protein (UniProt P00560 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1FW8 2.3 Å, Circularly permuted phosphoglycerate kinase from yeast: pgk P72
3PGK 2.5 Å, The structure of yeast phosphoglycerate kinase at 0.25 nm resolution
9R9O 2.9 Å, Yeast 80S with nascent chain in complex with Ssb1-ADP in the S1 state
9R9P 3.0 Å, Yeast 80S with nascent chain in complex with Ssb1-ADP in the S2 state

Browse structure collections

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