1QQO: Hydrolase

Name: PDB 1QQO: E175S mutant of bovine 70 kilodalton heat shock protein
Published: 1999-09-15
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: hydrolase

E175S mutant of bovine 70 kilodalton heat shock protein. Determined by X-ray diffraction at 1.9 Å resolution. Released 15 Sept 1999.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Bos taurus
Chains: 1
Atoms: 3,358
Mol. weight: 42.05 kDa
Ligands: ADP, MG
Released: 15 Sept 1999

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

Secondary structure: helices and β-sheets

1QQO contains 16 α-helices and 19 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: 16 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	7-11	5	1
β-strand	15-22	8	1
β-strand	25-28	4	1
α-helix	29-30	2
β-strand	38-39	2	1
β-strand	42-44	3	2
β-strand	49-51	3	2
α-helix	53-56	4
β-strand	66-67	2	2
α-helix	70-72	3
α-helix	81-87	7
β-strand	93-97	5	3
β-strand	100-107	8	3
β-strand	110-114	5	3
α-helix	116-135	20
β-strand	141-146	6	1
α-helix	152-164	13
β-strand	168-174	7	1
α-helix	175-182	8
β-strand	193-200	8	4
β-strand	205-213	9	4
β-strand	216-225	10	4
α-helix	230-249	20
α-helix	257-274	18
β-strand	279-288	10	5
β-strand	291-298	8	5
α-helix	299-312	14
α-helix	314-323	10
α-helix	328-330	3
β-strand	333-337	5	4
α-helix	339-342	4
α-helix	344-353	10
α-helix	357-359	3
β-strand	360	1	4
α-helix	368-380	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Hydrolase (acting on acid anhydrides)	A	protein	378	Bos taurus	P19120 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1QQO_1 HYDROLASE (ACTING ON ACID ANHYDRIDES) (chains A)
GPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNP
TNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMV
LTKMKEIAEAYLGATVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINSPTAAAIAY
GLDKAVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIA
EFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFE
ELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSI
NPDEAVAYGAAVQAAILS

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	1
MG	Magnesium ion	Mg	1

Water and common crystallization additives (K, CL) are not listed.

Primary citation

Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein. Johnson, E.R., McKay, D.B. Biochemistry (1999) 38:10823-10830. DOI 10.1021/bi990816g · PubMed

Other PDB entries of the same protein (UniProt P19120 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7ODB 1.66 Å, Crystal structure of bovine Hsc70(aa1-554)E213A/D214A in complex with triazine-derivative
1BA1 1.7 Å, Heat-shock cognate 70KD protein 44KD atpase N-terminal mutant with cys 17 replaced by lys
1BUP 1.7 Å, T13S mutant of bovine 70 kilodalton heat shock protein
1HPM 1.7 Å, How potassium affects the activity of the molecular chaperone HSC70. II. Potassium binds…
1KAX 1.7 Å, 70KD heat shock cognate protein atpase domain, K71M mutant
1KAY 1.7 Å, 70KD heat shock cognate protein atpase domain, K71A mutant
1KAZ 1.7 Å, 70KD heat shock cognate protein atpase domain, K71E mutant
2BUP 1.7 Å, T13G Mutant of the ATPASE fragment of Bovine HSC70
2QWO 1.7 Å, Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C…
2QWL 1.75 Å, Crystal structure of bovine hsc70 (1-394aa)in the ADP state
2QWP 1.75 Å, Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C…
7ODI 1.83 Å, Crystal structure of bovine Hsc70(aa1-554)E213A/D214A in complex with methanesulfonamide

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