Structure of PDB 3iuc Chain C

Receptor sequence
>3iucC (length=388) Species: 9606 (Homo sapiens) [Search protein sequence]
NLYFQSMDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAF
TPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFK
VVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHA
VVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKGEKNI
LVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLY
KKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSE
TLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPK
IQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGD
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
ChainC
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D34 S40 F68 T69 E201 D224
Catalytic site (residue number reindexed from 1) D16 S22 F50 T51 E183 D204
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 C T37 T38 Y39 G226 G227 E293 K296 R297 S300 G364 S365 R367 T19 T20 Y21 G206 G207 E273 K276 R277 S280 G344 S345 R347
BS02 CA C H252 D257 H232 D237
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)

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