Structure of PDB 1hjo Chain A

Receptor sequence
>1hjoA (length=380) Species: 9606 (Homo sapiens) [Search protein sequence]
KAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIG
DAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPK
VQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFND
SQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGG
GTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKD
ISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARF
EELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQD
FFNGRDLNKSINPDEAVAYGAAVQAAILMG
3D structure
PDB1hjo Structure of a new crystal form of human Hsp70 ATPase domain.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D10 K71 E175 D199
Catalytic site (residue number reindexed from 1) D8 K69 E173 D197
Enzyme Commision number 3.6.1.3: Deleted entry.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 ADP A G12 T13 T14 Y15 G201 G202 G230 E268 K271 R272 S275 G339 S340 R342 G10 T11 T12 Y13 G199 G200 G228 E266 K269 R270 S273 G337 S338 R340
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0140662 ATP-dependent protein folding chaperone

View graph for
Molecular Function
External links
PDB RCSB:1hjo, PDBe:1hjo, PDBj:1hjo
PDBsum1hjo
PubMed10216320
UniProtP0DMV8|HS71A_HUMAN Heat shock 70 kDa protein 1A (Gene Name=HSPA1A)

[Back to BioLiP]