Structure of PDB 4h5r Chain A

Receptor sequence
>4h5rA (length=382) Species: 9606 (Homo sapiens) [Search protein sequence]
KGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIG
DAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPK
VQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFND
SQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGG
GTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKD
ISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARF
EELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQD
FFNGKELNKSINPDEAVAYGAAVQAAILSGDK
3D structure
PDB4h5r New crystal structures of HSC-70 ATP binding domain confirm the role of individual binding pockets and suggest a new method of inhibition.
ChainA
Resolution1.64 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 3.6.4.10: non-chaperonin molecular chaperone ATPase.
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 PO4 A G12 T13 K71 E175 T204 G10 T11 K69 E173 T202
BS02 PO4 A I297 T298 R301 I295 T296 R299
BS03 PO4 A E255 N256 Y288 E253 N254 Y286
BS04 PO4 A K159 R171 I172 K157 R169 I170
BS05 GOL A T13 K71 Y149 F150 T226 T11 K69 Y147 F148 T224
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0140662 ATP-dependent protein folding chaperone

View graph for
Molecular Function
External links
PDB RCSB:4h5r, PDBe:4h5r, PDBj:4h5r
PDBsum4h5r
PubMed25433210
UniProtP11142|HSP7C_HUMAN Heat shock cognate 71 kDa protein (Gene Name=HSPA8)

[Back to BioLiP]