Structure of PDB 3iuc Chain A

Receptor sequence
>3iucA (length=379) Species: 9606 (Homo sapiens) [Search protein sequence]
GTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIG
DAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPY
IQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFN
DAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGG
GTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKD
VRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKF
EELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKE
FFNGKEPSRGINPDEAVAYGAAVQAGVLS
3D structure
PDB3iuc Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78
ChainA
Resolution2.4 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 S40 F68 T69 K96 E201 D224
Catalytic site (residue number reindexed from 1) D7 S13 F41 T42 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 ADP A T37 T38 Y39 G226 G227 G255 E293 K296 R297 S300 G364 S365 R367 T10 T11 Y12 G199 G200 G228 E266 K269 R270 S273 G337 S338 R340 PDBbind-CN: -logKd/Ki=5.66,Kd=2.17uM
BS02 CA A H252 D257 H225 D230
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0140662 ATP-dependent protein folding chaperone

View graph for
Molecular Function
External links
PDB RCSB:3iuc, PDBe:3iuc, PDBj:3iuc
PDBsum3iuc
PubMed20072699
UniProtP11021|BIP_HUMAN Endoplasmic reticulum chaperone BiP (Gene Name=HSPA5)

[Back to BioLiP]