Structure of PDB 3d2e Chain C

Receptor sequence
>3d2eC (length=627) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
STPFGLDLGNNNSVLAVARNRGIDIVVNEVSNRSTPSVVGFGPKNRYLGE
TGKNKQTSNIKNTVANLKRIIGLDYHHPDFEQESKHFTSKLVELDDKKTG
AEVRFAGEKHVFSATQLAAMFIDKVKDTVKQDTKANITDVCIAVPPWYTE
EQRYNIADAARIAGLNPVRIVNDVTAAGVSYGIFKTDLPEGEEKPRIVAF
VDIGHSSYTCSIMAFKKGQLKVLGTACDKHFGGRDFDLAITEHFADEFKT
KYKIDIRENPKAYNRILTAAEKLKKVLSANTNAPFSVESVMNDVDVSSQL
SREELEELVKPLLERVTEPVTKALAQAKLSAEEVDFVEIIGGTTRIPTLK
QSISEAFGKPLSTTLNQDEAIAKGAAFICAIHSPTLRVRPFKFEDIHPYS
VSYSWDKQVEDEDHMEVFPAGSSFPSTKLITLNRTGDFSMAASYTDITQL
PPNTPEQIANWEITGVQLPEGQDSVPVKLKLRCDPSGLHTIEEAYTIKTV
KKDDLTIVAHTFGLDAKKLNELIEKENEMLAQDKLVAETEDRKNTLEEYI
YTLRGKLEEEYAPFASDAEKTKLQGMLNKAEEWLYDEGFDSIKAKYIAKY
EELASLGNIIRGRYLAKEEEKKQAIRS
3D structure
PDB3d2e Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding.
ChainC
Resolution2.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D8 K69 D174 D203
Catalytic site (residue number reindexed from 1) D7 K68 D173 D202
Enzyme Commision number ?
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 C G10 N11 N12 N13 K69 G205 H206 S207 E272 K275 K276 S279 G342 G343 T344 R346 G9 N10 N11 N12 K68 G204 H205 S206 E271 K274 K275 S278 G341 G342 T343 R345
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0140662 ATP-dependent protein folding chaperone

View graph for
Molecular Function
External links
PDB RCSB:3d2e, PDBe:3d2e, PDBj:3d2e
PDBsum3d2e
PubMed18555782
UniProtP32589|HSP7F_YEAST Heat shock protein homolog SSE1 (Gene Name=SSE1)

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