1HX1: Bag domain

Crystal structure of a bag domain in complex with the HSC70 atpase domain. Determined by X-ray diffraction at 1.9 Å resolution. Released 7 Mar 2001.

Method: X-ray diffraction
Resolution: 1.9 Å
Organisms: Bos taurus, Homo sapiens
Chains: 2
Atoms: 4,143
Mol. weight: 57.79 kDa
Released: 7 Mar 2001

Explore 1HX1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1HX1 contains 22 α-helices and 19 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: 18 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
β-strand	38-39	2	1
β-strand	42-44	3	2
β-strand	49-51	3	2
α-helix	53-57	5
α-helix	59-61	3
α-helix	63-65	3
β-strand	66-67	2	2
α-helix	70-72	3
α-helix	81-86	6
α-helix	87-89	3
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	175-183	9
β-strand	193-201	9	4
β-strand	204-213	10	4
β-strand	216-225	10	4
α-helix	230-249	20
α-helix	257-273	17
β-strand	279-288	10	5
β-strand	291-298	8	5
α-helix	299-305	7
α-helix	307-312	6
α-helix	314-323	10
α-helix	328-330	3
β-strand	333-337	5	4
α-helix	339-342	4
α-helix	344-351	8
β-strand	360	1	4
α-helix	368-380	13

Chain B: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	153-188	36
α-helix	193-201	9
α-helix	204-221	18
α-helix	231-255	25

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Heat shock 70 kDa protein 8	A	protein	400	Bos taurus	P19120 (AlphaFold model)
BAG family molecular chaperone regulator 1	B	protein	114	Homo sapiens	Q99933 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1HX1_1 Heat shock 70 kDa protein 8 (chains A)
MSYYHHHHHHDYDPTTENLYFQGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSY
VAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRP
KVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDA
GTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKS
TAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQAS
IEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGST
RIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILS

Sequence of entity 2 (B), FASTA

>1HX1_2 BAG family molecular chaperone regulator 1 (chains B)
GNSPQEEVELKKLKHLEKSVEKIADQLEELNKELTGIQQGFLPKDLQAEALCKLDRRVKA
TIEQFMKILEEIDTLILPENFKDSRLKRKGLVKKVQAFLAECDTVEQNICQETE

Primary citation

Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Sondermann, H., Scheufler, C., Schneider, C. et al. Science (2001) 291:1553-1557. DOI 10.1126/science.1057268 · 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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