3HPR: V148G adenylate kinase from E. coli

Crystal structure of V148G adenylate kinase from E. coli, in complex with Ap5A. Determined by X-ray diffraction at 2.0 Å resolution. Released 3 Nov 2009.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Escherichia coli
Chains: 2
Atoms: 3,829
Mol. weight: 48.99 kDa
Ligands: AP5
Released: 3 Nov 2009

Explore 3HPR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3HPR contains 30 α-helices and 22 β-strands across 2 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: 14 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	1
α-helix	13-24	12
β-strand	28-30	3	1
α-helix	31-41	11
α-helix	49-54	6
α-helix	57-60	4
α-helix	61-72	12
α-helix	75-77	3
β-strand	81-84	4	1
α-helix	90-98	9
β-strand	105-110	6	1
α-helix	113-121	9
β-strand	123-126	4	2
β-strand	131-134	4	2
β-strand	138	1	2
β-strand	145	1	3
α-helix	151	1
β-strand	152	1	3
α-helix	153	1
β-strand	154	1	2
α-helix	161-170	10
α-helix	171-175	5
α-helix	177-187	11
β-strand	192-197	6	1
α-helix	202-213	12

Chain B: 16 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	4
α-helix	13-24	12
β-strand	28-30	3	4
α-helix	31-41	11
α-helix	47-49	3
α-helix	50-54	5
α-helix	57-60	4
α-helix	61-72	12
α-helix	75-77	3
β-strand	81-84	4	4
α-helix	90-99	10
β-strand	105-110	6	4
α-helix	113-115	3
α-helix	116-121	6
β-strand	123-126	4	5
β-strand	131-134	4	5
β-strand	138	1	5
β-strand	145	1	6
α-helix	151	1
β-strand	152	1	6
α-helix	153	1
β-strand	154	1	5
α-helix	161-170	10
α-helix	171-175	5
α-helix	177-187	11
β-strand	192-197	6	4
α-helix	202-213	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Adenylate kinase	A, B	protein	214	Escherichia coli	P69441 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3HPR_1 Adenylate kinase (chains A, B)
MRIILLGAPGAGKGTQAQFIMEKYGIPQISTGDMLRAAVKSGSELGKQAKDIMDAGKLVT
DELVIALVKERIAQEDCRNGFLLDGFPRTIPQADAMKEAGINVDYVLEFDVPDELIVDRI
VGRRVHAPSGRVYHVKFNPPKVEGKDDGTGEELTTRKDDQEETVRKRLVEYHQMTAPLIG
YYSKEAEAGNTKYAKVDGTKPVAEVRADLEKILG

Ligands and cofactors

ID	Name	Formula	Copies
AP5	Bis(adenosine)-5'-pentaphosphate	C20 H29 N10 O22 P5	2

Primary citation

Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins. Schrank, T.P., Bolen, D.W., Hilser, V.J. Proc Natl Acad Sci U S A (2009) 106:16984-16989. DOI 10.1073/pnas.0906510106 · PubMed

Other PDB entries of the same protein (UniProt P69441 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7APU 1.36 Å, Structure of Adenylate kinase from Escherichia coli in complex with two ADP molecules…
6F7U 1.4 Å, Molecular Mechanism of ATP versus GTP Selectivity of Adenylate Kinase
8CRG 1.49 Å, E. coli adenylate kinase in complex with two ADP molecules as a result of enzymatic AP4A…
8RJ9 1.59 Å, E. coli adenylate kinase Asp84Ala variant in complex with two ADP molecules as a result…
6S36 1.6 Å, Crystal structure of E. coli Adenylate kinase R119K mutant
9R71 1.61 Å, Crystal structure of E. coli Adenylate kinase E114A mutant in complex with inhibitor Ap5a.
6RZE 1.69 Å, Crystal structure of E. coli Adenylate kinase R119A mutant
4X8L 1.7 Å, Crystal structure of E. coli Adenylate kinase P177A mutant in complex with inhibitor Ap5a
8Q2B 1.76 Å, E. coli Adenylate Kinase variant D158A (AK D158A) showing significant changes to the…
9R6U 1.77 Å, Crystal structure of E. coli Adenylate kinase K47A mutant in complex with inhibitor Ap5A
1E4V 1.85 Å, Mutant G10V of adenylate kinase from E. coli, modified in the Gly-loop
1E4Y 1.85 Å, Mutant P9L of adenylate kinase from E. coli, modified in the Gly-loop

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