Structure of PDB 5f1x Chain A

Receptor sequence
>5f1xA (length=380) Species: 9606 (Homo sapiens) [Search protein sequence]
DVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERL
IGDAAKNQSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPY
IQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFN
DAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGG
GTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKD
VRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKF
EELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKE
FFNGKEPSRGINPDEAVAYGAAVQAGVLSG
3D structure
PDB5f1x Probing the ATP Site of GRP78 with Nucleotide Triphosphate Analogs.
ChainA
Resolution1.9 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) D34 K96 E201 D224
Catalytic site (residue number reindexed from 1) D9 K69 E174 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 ATP A G36 T37 T38 Y39 G226 G227 G228 T229 G255 E293 K296 R297 S300 G363 G364 R367 G11 T12 T13 Y14 G199 G200 G201 T202 G228 E266 K269 R270 S273 G336 G337 R340 MOAD: Kd=0.000000064M
PDBbind-CN: -logKd/Ki=6.11,Kd=780nM
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0140662 ATP-dependent protein folding chaperone

View graph for
Molecular Function
External links
PDB RCSB:5f1x, PDBe:5f1x, PDBj:5f1x
PDBsum5f1x
PubMed27144892
UniProtP11021|BIP_HUMAN Endoplasmic reticulum chaperone BiP (Gene Name=HSPA5)

[Back to BioLiP]